ATTORNEY DOCKET: 51494-029WO2 PATENT COMPOSITIONS AND METHODS FOR THE PRODUCTION OF POLYURETHANES Background of the Invention Finding sustainable biomass sources that may be used for the development of new biomaterials without the need for petroleum-derived materials is an important component in developing a circular and sustainable economy. However, most of these sources are of plant origin and, therefore, compete with food production, requiring cropland, water, and harvesting. It has been recently shown that by-products of synthetic biology, particularly those recovered by distillation, may be able to play a role in developing new biomaterials, as they contain polyols compatible with biopolymer manufacture. However, such by- products are not presently suitable for use, as they are mixed with other degradation by-products, making their use impractical. Therefore, the valorization of secondary materials from fermentation processes represents an opportunity to access valuable starting materials for the development of novel, bio-based polymers with useful properties. These bio-based polymers can be applied in many fields, such as packaging, automotive coatings and/or adhesives, biomedical devices, and household products, among others. However, to access these resources, there remains a need for processes that efficiently isolate secondary materials from a fermentation mixture. Summary of the Invention The present disclosure provides compositions and methods for synthesizing polymers (e.g., polyurethanes and polyurethane-based renewable resources), particularly from residue produced as a by- product of host cells (e.g., yeast cells) that are capable of producing a fermentation product. The compositions and methods described herein provide a significant benefit to the field of synthetic biology: the ability to sustainably produce new materials using components found in by-products of fermentation. For example, polyols, which have been identified as being of potential interest in producing new materials, may be found in the by-products of fermentation, particularly in the residue (e.g., distillate residue) from a fermentation composition. However, isolating the polyols such that they are suitable for synthesis (e.g., by way of polymerization) has been a significant challenge. In order to access the polyols found in the residue of a fermentation composition, the various impurities (e.g., wax, sludge, and other degradation by-products) that are also found in the residue of a fermentation composition must be successfully removed. The present disclosure is based, in part, on the discovery of processes capable of isolating fermentation by-products, such as polyols, in a manner that renders these by-products suitable for the synthesis of biopolymers. Using a unique combination of extraction, distillation, and reaction steps described herein, one can produce bio-based polymer (e.g., polyurethane) compositions. The sections that follow provide a description of the compositions and methods that can be used to obtain polymer materials starting from residues resulting from a fermentation process. In a first aspect, the disclosure provides a method of synthesizing a polyurethane from a fermentation composition that has been produced by culturing a population of host cells capable of producing a fermentation product in a culture medium and under conditions suitable for the host cells to produce the fermentation product. The method includes: (a) extracting an oil fraction obtained from a ATTORNEY DOCKET: 51494-029WO2 PATENT residue from the fermentation composition; (b) distilling the oil fraction of step (a), thereby producing a distillation product; and (c) reacting the distillation product of step (b) with an isocyanate to form the polyurethane. In some embodiments, the residue is a distillate residue. In some embodiments, the extracting includes a winterization step and/or a filtration step. In some embodiments, the winterization step includes dissolving the residue (e.g., distillate residue) from a fermentation composition in ethanol. In some embodiments, the ethanol is added to a concentration of 1:4 (w:v) of residue (e.g., distillate residue) from the fermentation composition to ethanol, thereby forming an ethanol solution. In some embodiments, the ethanol solution is mixed for between about 1 minute and about 1 hour (e.g., between about 10 minutes and 1 hour, 20 minutes and 1 hour, 30 minutes and 1 hour, 40 minutes and 1 hour, 50 minutes and 1 hour, 1 minute and 50 minutes, 1 minute and 40 minutes, 1 minute and 30 minutes, 1 minute and 20 minutes, or 1 minute and 10 minutes). In some embodiments, the ethanol solution is mixed for between about 1 minute and about 20 minutes (e.g., 1 minute, 2 minutes, 3 minutes, 4 minutes, 5 minutes, 6 minutes, 7 minutes, 8 minutes, 9 minutes, 10 minutes, 11 minutes, 12 minutes, 13 minutes, 14 minutes, 15 minutes, 16 minutes, 17 minutes, 18 minutes, 19 minutes, or 20 minutes). In some embodiments, the ethanol solution is mixed for about 5 minutes. In some embodiments, the ethanol solution is let stand for between about 10 minutes and about 6 hours (e.g., between about 10 minutes and 5 hours, 10 minutes and 4 hours, 10 minutes and 3 hours, 10 minutes and 2 hours, 10 minutes and 1 hour, 1 hour and 6 hours, 2 hours and 6 hours, 3 hours and 6 hours, 4 hours and 6 hours, or 5 hours and 6 hours). In some embodiments, the ethanol solution is let stand for between about 1 hour and about 3 hours (e.g., between about 60 minutes and about 90 minutes, about 60 minutes and about 2 hours, about 60 minutes and about 150 minutes, or about 60 minutes and about 2 hours). In some embodiments, the ethanol solution is let stand for about 2 hours. In some embodiments, the ethanol solution is let stand at about room temperature. In some embodiments, the ethanol solution is chilled for between about 1 hour and about 24 hours (e.g., between 1 hour and 18 hours, 1 hour and 12 hours, 1 hour and 6 hours, 6 hours and 24 hours, 12 hours and 24 hours, 18 hours and 24 hours, or 6 hours and 18 hours. In some embodiments, the ethanol solution is chilled for between 8 hours and 16 hours (e.g., 8 hours, 9 hours, 10 hours, 11 hours, 12 hours, 13 hours, 14 hours, 15 hours, or 16 hours. In some embodiments, the ethanol solution is chilled at a temperature of between about -50 ^o C and about 0 ^o C (e.g., between about -40 ^o C and 0 ^o C, -30 ^o C and 0 ^o C, -20 ^o C and 0 ^o C, -10 ^o C and 0 ^o C, and -30 ^o C and -10 ^o C). In some embodiments, the ethanol solution is chilled to a temperature of between about -40 ^o C and about -20 ^o C (e.g., about -40 ^o C, -35 ^o C, -30 ^o C, -25 ^o C, or -20 ^o C). In some embodiments, the ethanol solution is chilled to a temperature of about -30 ^o C. In some embodiments, the winterization step further includes centrifugation of the ethanol solution. In some embodiments, the ethanol solution is centrifuged at a speed of between about 500 g and about 2000 g (e.g., between about 500 g and 1500 g, 500 g and 1000 g, 1000 g, and 2000 g, 1500 g and 2000 g, or 1000 g and 1500 g). In some embodiments, the ethanol solution is centrifuged at a speed of between about 1000 g and about 1500 g (e.g., between about 1000 g and 1400 g, 1000 g and 1300 g, 1000 g and 1200 g, 1000 g and 1100 g, 1100 g and 1500 g, 1200 g and 1500 g, 1300 g and 1500 g, or ATTORNEY DOCKET: 51494-029WO2 PATENT 1400 g and 1500 g). In some embodiments, the centrifugation of the ethanol solution is performed at a speed of about 1250 g. In some embodiments, the ethanol solution is centrifuged for between about 1 minute and about 30 minutes (e.g., between about 1 minute and about 20 minutes, about 1 minute and about 10 minutes, about 1 minute and about 5 minutes, about 5 minutes and about 20 minutes, about 10 minutes and about 20 minutes, or about 15 minutes and about 20 minutes). In some embodiments, the ethanol solution is centrifuged at about room temperature. In some embodiments, the filtration step includes at least 2 filtration steps. In some embodiments, the method includes between 2 and 5 filtration steps (e.g., 2 filtration steps, 3 filtration steps, 4 filtration steps, or 5 filtration steps). In some embodiments, the method includes a first filtration step, a second filtration step, and a third filtration step. In some embodiments, the first filtration step includes filtering the residue (e.g., distillate residue) from a fermentation composition through a nonwoven (TNT) filter. In some embodiments, the second filtration step includes filtering through a filter having a membrane that is between 5 µm and 15 µm in pore size (e.g., about 5 µm, 6 µm, 7 µm, 8 µm, 9 µm, 10 µm, 11 µm, 12 µm, 13 µm, 14 µm, or 15 µm in pore size). In some embodiments, the membrane is about 11 µm. In some embodiments, the third filtration step includes filtering through a filter having a membrane that is between 5 µm and 15 µm in pore size (e.g., about 5 µm, 6 µm, 7 µm, 8 µm, 9 µm, 10 µm, 11 µm, 12 µm, 13 µm, 14 µm, or 15 µm in pore size). In some embodiments, the membrane is about 8 µm in pore size. In some embodiments, the filtration step is performed under vacuum. In some embodiments, the distilling includes short path distillation. In some embodiments, the distilling is performed at temperature of between about 125 ^o C and about 250 ^o C (e.g., between 150 ^o C and 250 ^o C, 175 ^o C and 250 ^o C, 200 ^o C and 250 ^o C, 225 ^o C and 250 ^o C, 125 ^o C and 225 ^o C, 125 ^o C and 200 ^o C, 125 ^o C and 175 ^o C, or 125 ^o C and 150 ^o C). In some embodiments, the distilling is performed at a temperature of between 150 ^o C and 225 ^o C (e.g., between 150 ^o C and 200 ^o C, 150 ^o C and 175 ^o C, 175 ^o C and 225 ^o C, 200 ^o C and 225 ^o C, or 170 ^o C and 210 ^o C). In some embodiments, the distilling is performed at a temperature of between 170 ^o C and 190 ^o C (e.g., 170 ^o C, 171 ^o C, 172 ^o C, 173 ^o C, 174 ^o C, 175 ^o C, 176 ^o C, 178 ^o C, 179 ^o C, 180 ^o C, 181 ^o C, 182 ^o C, 183 ^o C, 184 ^o C, 185 ^o C, 186 ^o C, 187 ^o C, 188 ^o C, 189 ^o C, or 190 ^o C). In some embodiments, the distilling is performed at a temperature of about 180 ^o C. In some embodiments, the distilling is performed at a pressure of between about 0.01 mbar and about 1 mbar (e.g., between about 0.01 mbar and about 0.75 mbar, about 0.01 mbar and about 0.5 mbar about 0.01 mbar and about 0.25 mbar, about 0.01 mbar and about 0.1 mbar, about 0.01 mbar and about 0.05 mbar, about 0.05 mbar and about 1 mbar, about 0.1 mbar and about 1 mbar, about 0.25 mbar and about 1 mbar, about 0.5 mbar and about 1 mbar, or about 0.75 mbar and about 1 mbar). In some embodiments, the distilling is performed at a pressure of between about 0.05 mbar and about 0.5 mbar (e.g., between about 0.05 mbar and about 0.4 mbar, about 0.05 mbar and about 0.3 mbar, about 0.05 mbar and about 0.2 mbar, about 0.05 mbar and about 0.1 mbar, about 0.1 mbar and about 0.5 mbar, about 0.2 mbar and about 0.5 mbar, about 0.3 mbar and about 0.5 mbar, or about 0.4 mbar and about 0.5 mbar). In some embodiments, the distilling is performed at a temperature of about 0.1 mbar. In some embodiments, the distilling is performed at a feed rate of between about 0.5 mL/min and about 2.5 mL/min (e.g., between about 1 mL/min and about 2.5 mL/min, about 1.5 mL/min and about 2.5 mL/min, about 2 mL/min and about 2.5 mL/min, about 0.5 mL/min and about 2 mL/min, about 1 mL/min ATTORNEY DOCKET: 51494-029WO2 PATENT and about 2 mL/min, or about 1.5 mL/min and about 2 mL/min). In some embodiments, the distillation step is performed at a feed rate of between about 1 mL/min and about 2 mL/min (e.g., about 1.1 mL/min, 1.2 mL/min, 1.3 mL/min, 1.4 mL/min, 1.5 mL/min, 1.6 mL/min, 1.7 mL/min, 1.8 mL/min, 1.9 mL/min, or 2 mL/min). In some embodiments, distillation step is performed at a feed rate of about 1.5 mL/min. In some embodiments, the distilling is performed at a rotor rate of between about 100 rpm and 500 rpm (e.g., between about 100 rpm and about 400 rpm, about 100 rpm and about 300 rpm, about 100 rpm and about 200 rpm, about 200 rpm and about 500 rpm, about 300 rpm and about 500 rpm, or about 400 rpm and about 500 rpm). In some embodiments, the reacting step includes contacting the distillation product of step (b) with the isocyanate. In some embodiments, the distillation product is hydroxylated. In some embodiments, the distillation product is a polyol. In some embodiments, the distillation product of step (b) and the isocyanate are reacted in a ratio of between about 5:1 (w/w) and about 1:5 (w/w) (e.g., about 3:1 (w/w) and about 1:5 (w/w), about 1:1 (w/w) and about 1:5 (w/w), about 1:2 (w/w) and about 1:5 (w/w), about 5:1 (w/w) and about 1:2 (w/w), about 5:1 (w/w) and about 1:1 (w/w), about 5:1 (w/w) and about 2:1(w/w), or about 5:1 (w/w) and about 4:1 (w/w)). In some embodiments, the distillation product of step (b) and the isocyanate are reacted in a ratio of between about 3:1 (w/w) and about 1:1 (w/w) (e.g., about 3:1 (w/w), about 2:1 (w/w), or about 1:1 (w/w)). In some embodiments, the distillation product of step (b) and the isocyanate are reacted in a ratio of about 7:3 (w/w). In some embodiments, the isocyanate includes one or more of toluene diisocyanate (TDI), methylenediphenyl diisocyanate (MDI), hexamethylene diisocyanate (HDI), or isophorone diisocyanate (IPDI). In some embodiments, the isocyanate includes TDI. In some embodiment, the isocyanate includes MDI. In some embodiments, the isocyanate includes HDI. In some embodiments, the isocyanate includes IPDI. In some embodiments, the reacting step further includes contacting the distillation product of step (b) with vinyltrimethoxy silane. In some embodiments, the vinyltrimethoxy silane has a final concentration of between about 1% (w/v) and about 3% (w/v) (e.g., between about 1% (w/v) and about 2.5% (w/v), about 1% (w/v) and 2% (w/v), about 1% (w/v) and 1.5% (w/v), about 1.5% (w/v) and 3% (w/v), about 2% (w/v) and 3% (w/v), or about 2.5% (w/v) and 3% (w/v)). In some embodiments, the vinyltrimethoxy silane has a final concentration of about 2% (w/v). In some embodiments, the reacting step further includes contacting the distillation product of step (b) with a catalyst. In some embodiments, the catalyst is dibutyltin dilaurate. In some embodiments, the catalyst has a final concentration of between about 0.05% (w/v) and about 1% (w/v) (e.g., about 0.1% (w/v) and about 1% (w/v), about 0.5% (w/v) and about 1, about 0.75% (w/v) and about 0.1% (w/v 1% (w/v), 0.05% (w/v) and about 0.75% (w/v), about 0.05% (w/v) and about 0.5% (w/v), or about 0.05% (w/v) and about 0.1% (w/v)). In some embodiments, the catalyst is present in a final concentration of between about 0.1% (w/v) and about 0.5% (w/v) (e.g., about 0.1% (w/v), about 0.2% (w/v), about 0.3% (w/v), about 0.4% (w/v), or about 0.5% (w/v)). In some embodiments, the catalyst is present in a final concentration of 0.2% (w/v). In some embodiments, the reacting of the distillation product of step (b) with the isocyanate is performed at a temperature of between about 25 ^o C and about 100 ^o C (e.g., between about 25 ^o C and about 75 ^o C, about 25 ^o C and about 50 ^o C, about 50 ^o C and about 100 ^o C, or about 75 ^o C and about 100 ATTORNEY DOCKET: 51494-029WO2 PATENT ^o C). In some embodiments, the reacting step is performed at a temperature of between about 50 ^o C and about 90 ^o C (e.g., between about 50 ^o C and about 80 ^o C, about 50 ^o C and about 70 ^o C, about 50 ^o C and about 60 ^o C, about 60 ^o C and about 90 ^o C, about 70 ^o C and about 90 ^o C, or about 80 ^o C and about 90 ^o C). In some embodiments, the reacting step is performed at a temperature of about 70 ^o C. In some embodiments, the reacting of the distillation product of step (b) with the isocyanate is performed for between about 12 hours and about 72 hours (e.g., between about 12 hours and about 60 hours, about 12 hours and about 48 hours, about 12 hours and about 36 hours, about 12 hours and about 24 hours, about 24 hours and about 72 hours, about 36 hours and about 72 hours, about 48 hours and about 72 hours, or about 60 hours and about 72 hours). In some embodiments, the reacting of the distillation product with the isocyanate is performed for between about 36 hours and about 60 hours (e.g., between about 42 hours and about 60 hours, about 48 hours and about 60 hours, about 54 hours and about 60 hours, about 36 hours and about 54 hours, about 36 hours and about 48 hours, or about 36 hours and about 42 hours). In some embodiments, reacting of the distillation product with the isocyanate is performed for about 48 hours. In some embodiments, the fermentation product is an isoprene. In some embodiments, the fermentation product is an isoprenoid. In some embodiments, the fermentation product is β-farnesene. In some embodiments, the fermentation product is a steviol glycoside. In some embodiments, the fermentation product is a human milk oligosaccharide. In some embodiments, the fermentation product is a cannabinoid. In some embodiments, the host cell is a yeast cell. In some embodiments, the yeast cell is S. Cerevisiae. In some embodiments, the polyurethane has elongation at break of between about 20% and about 1000% (e.g., between about 20% and about 800%, about 20% and about 600%, about 20% and about 400%, about 20% and about 200%, about 20% and about 50%, about 50% and about 1000%, about 200% and about 1000%, about 400% and about 1000%, about 600% and about 1000%, or about 800% and about 1000%). In some embodiments, the polyurethane has elongation at break of between about 50% and about 700% (e.g., about 50% and about 600%, about 50% and about 500%, about 50% and about 400%, about 50% and about 300%, about 50% and about 200%, about 50% and about 100%, about 100% and about 700%, about 200% and about 700%, about 300% and about 700%, about 400% and about 700%, about 500% and about 700%, or about 600% and about 700%). In some embodiments, the polyurethane has a Young modulus of between about 0.1 Mpa and about 4 Mpa (e.g., between about 0.1 Mpa and about 3 Mpa, about 0.1 Mpa and about 2 Mpa, about 0.1 Mpa and about 1 Mpa, about 0.1 Mpa and about 0.5 Mpa, about 0.5 Mpa and about 4 Mpa, about 1 Mpa and about 4 Mpa, about 2 Mpa and about 4 Mpa, or about 3 Mpa and about 4 Mpa). In some embodiments, the polyurethane has a Young modulus of between about 0.2 Mpa and about 3.5 Mpa (e.g., between about 0.2 Mpa and about 3 Mpa, about 0.2 Mpa and about 2.5 Mpa, about 0.2 Mpa and about 2 Mpa, about 0.2 Mpa and about 1.5 Mpa, about 0.2 Mpa and about 1 Mpa, about 0.2 Mpa and about 0.5 Mpa, about 0.5 Mpa and about 3.5 Mpa, about 1 Mpa and about 3.5 Mpa, about 1.5 Mpa and about 3.5 Mpa, about 2 Mpa and about 3.5 Mpa, about 2.5 Mpa and about 3.5 Mpa, or about 3 Mpa and about 3.5 Mpa). In another aspect, the disclosure provides a composition including a polyurethane, wherein the composition is produced by any one of the methods provided herein. In some embodiments, the ATTORNEY DOCKET: 51494-029WO2 PATENT polyurethane has elongation at break of between about 20% and about 1000% (e.g., between about 20% and about 800%, about 20% and about 600%, about 20% and about 400%, about 20% and about 200%, about 20% and about 50%, about 50% and about 1000%, about 200% and about 1000%, about 400% and about 1000%, about 600% and about 1000%, or about 800% and about 1000%). In some embodiments, the polyurethane has elongation at break of between about 50% and about 700% (e.g., about 50% and about 600%, about 50% and about 500%, about 50% and about 400%, about 50% and about 300%, about 50% and about 200%, about 50% and about 100%, about 100% and about 700%, about 200% and about 700%, about 300% and about 700%, about 400% and about 700%, about 500% and about 700%, or about 600% and about 700%). In some embodiments, the polyurethane has a Young modulus of between about 0.1 Mpa and about 4 Mpa (e.g., between about 0.1 Mpa and about 3 Mpa, about 0.1 Mpa and about 2 Mpa, about 0.1 Mpa and about 1 Mpa, about 0.1 Mpa and about 0.5 Mpa, about 0.5 Mpa and about 4 Mpa, about 1 Mpa and about 4 Mpa, about 2 Mpa and about 4 Mpa, or about 3 Mpa and about 4 Mpa). In some embodiments, the polyurethane has a Young modulus of between about 0.2 Mpa and about 3.5 Mpa (e.g., between about 0.2 Mpa and about 3 Mpa, about 0.2 Mpa and about 2.5 Mpa, about 0.2 Mpa and about 2 Mpa, about 0.2 Mpa and about 1.5 Mpa, about 0.2 Mpa and about 1 Mpa, about 0.2 Mpa and about 0.5 Mpa, about 0.5 Mpa and about 3.5 Mpa, about 1 Mpa and about 3.5 Mpa, about 1.5 Mpa and about 3.5 Mpa, about 2 Mpa and about 3.5 Mpa, about 2.5 Mpa and about 3.5 Mpa, or about 3 Mpa and about 3.5 Mpa). Definitions As used in this specification and the appended claims, the singular forms “a,” “an,” and “the” include plural reference unless the context clearly dictates otherwise. The term “about” when modifying a numerical value or range herein includes normal variation encountered in the field, and includes plus or minus 1-10% (e.g., 1%, 2%, 3%, 4%, 5%, 6%, 7%, 8%, 9% or 10%) of the numerical value or end points of the numerical range. Thus, a value of 10 includes all numerical values from 9 to 11. All numerical ranges described herein include the endpoints of the range unless otherwise noted, and all numerical values in-between the end points, to the first significant digit. As used herein, the term “cannabinoid” refers to a chemical substance that binds or interacts with a cannabinoid receptor (for example, a human cannabinoid receptor) and includes, without limitation, chemical compounds such endocannabinoids, phytocannabinoids, and synthetic cannabinoids. Synthetic compounds are chemicals made to mimic phytocannabinoids which are naturally found in the cannabis plant (e.g., Cannabis sativa), including but not limited to cannabigerols (CBG), cannabichromens (CBC), cannabidiol (CBD), tetrahydrocannabinol (THC), cannabinol (CBN), cannabinodiol (CBDL), cannabicyclol (CBL), cannabielsoin (CBE), and cannabitriol (CBT). As used herein, the term “capable of producing” refers to a host cell which includes the enzymes necessary for the production of a given compound in accordance with a biochemical pathway that produces the compound. For example, a cell (e.g., a yeast cell) that is “capable of producing” squalene is one that contains the enzymes necessary for production of the squalene according to the squalene biosynthetic pathway. ATTORNEY DOCKET: 51494-029WO2 PATENT As used herein, the term “distillation” describes a process by which at least a portion of a liquid undergoes a state change to have a gaseous state. For example, distillation may be used to separate two liquids from one another or to remove one liquid from a mixture containing one or more additional liquids. In some embodiments, evaporation includes the process of distillation, in which a liquid not only changes phase to a gaseous state, but is subsequently condensed back to a liquid form. In some embodiments of the disclosure, a distillation is performed by heating a mixture of liquids such that a lower-boiling point substance begins to evaporate, changing phase from a liquid to a gaseous state, while leaving the remaining liquid(s) in the mixture in a liquid phase. The lower-boiling point substance may then be condensed, e.g., upon exposure to reduced temperature, thereby: (1) returning the lower-boiling point substance to a liquid phase, and (2) separating the lower-boiling point substance from the remaining liquid(s) in the mixture. The distillation may be, for example, a “simple distillation,” which refers to a process in which a mixture of liquids having substantially different boiling points (e.g., boiling points that differ from one another by about 25 C ^o or more) is separated by heating the mixture until substantially all of the lower- boiling point substance evaporates and substantially all of the higher-boiling point substance remains in the liquid phase. The vapor of the lower-boiling point substance, in turn, is condensed so as to return the lower-boiling point substance to the liquid phase. In some embodiments, the distillation may be a “fractional distillation,” a process that is used, e.g., for separating highly miscible liquids and/or those having boiling points that differ by less than about 25 C ^o . A fractional distillation process involves heating a mixture containing the liquids such that the resulting vapor enters a fractionating column. The fractionating column is a column (e.g., a vertical, inclined, or horizontal column) configured so as to have a temperature gradient: the bottom of the fractionating column (i.e., the point at which the vapor enters the column) is the warmest, and the top of the fractionating column is the coolest. As the vapor proceeds upward through the column, the vapor is enriched for the lower-boiling point substance as a result of the temperature gradient. Once enriched for the lower-boiling point substance, the vapor exits the fractionating column and is exposed to a reduced temperature, thereby condensing the lower-boiling point substance and resolving the liquid mixture into its components. As used herein, the term “distillate residue” refers to material remaining after a composition (e.g., a fermentation composition including a population of host cells capable of producing a fermentation product and a culture medium) has undergone a distillation process. The term “distillate residue” includes residue that is left behind in a first vessel after a fermentation composition has undergone distillation, and the distillation product is now found in a second vessel. In some embodiments, the distillate residue may include a hydroxylated product or may include polyols. As used herein, the term “endogenous” describes a molecule (e.g., a polypeptide, nucleic acid, or cofactor) that is found naturally in a particular organism (e.g., a human) or in a particular location within an organism (e.g., an organ, a tissue, or a cell, such as a human cell). As used herein, the term “exogenous” describes a molecule (e.g., a polypeptide, nucleic acid, or cofactor) that is not found naturally in a particular organism (e.g., a human) or in a particular location within an organism (e.g., an organ, a tissue, or a cell, such as a human cell). Exogenous materials include those that are provided from an external source to an organism or to cultured matter extracted therefrom. ATTORNEY DOCKET: 51494-029WO2 PATENT As used herein in the context of a gene, the term “express” refers to any one or more of the following events: (1) production of an RNA template from a DNA sequence (e.g., by transcription); (2) processing of an RNA transcript (e.g., by splicing, editing, 5’ cap formation, and/or 3’ end processing); (3) translation of an RNA into a polypeptide or protein; and (4) post-translational modification of a polypeptide or protein. Expression of a gene of interest in a cell, tissue sample, or subject can manifest, for example, as: an increase in the quantity or concentration of mRNA encoding a corresponding protein (as assessed, e.g., using RNA detection procedures described herein or known in the art, such as quantitative polymerase chain reaction (qPCR) and RNA seq techniques), an increase in the quantity or concentration of a corresponding protein (as assessed, e.g., using protein detection methods described herein or known in the art, such as enzyme-linked immunosorbent assays (ELISA), among others), and/or an increase in the activity of a corresponding protein (e.g., in the case of an enzyme, as assessed using an enzymatic activity assay described herein or known in the art). As used herein, the term “fermentation composition” refers to a composition which contains host cells and products, or metabolites produced by the genetically modified host cells. An example of a fermentation composition is a whole cell broth, which may be the entire contents of a vessel, including cells, aqueous phase, and compounds produced from the host cells. As used herein, the term “fermentation product” refers to a compound that is produced by a host cell (e.g., yeast cell), which is cultured in a medium and under conditions suitable for the host cells to produce the fermentation product. The fermentation product may be naturally produced by the host cells or may be produced by host cells that have been genetically modified to produce the fermentation product. As used herein, the term “gene” refers to the segment of DNA involved in producing or encoding a polypeptide chain. It may include regions preceding and following the coding region (leader and trailer) as well as intervening sequences (introns) between individual coding segments (exons). Alternatively, the term “gene” can refer to the segment of DNA involved in producing or encoding a non-translated RNA, such as an rRNA, tRNA, gRNA, or micro RNA. A “genetic pathway” or “biosynthetic pathway” as used herein refers to a set of at least two different coding sequences, where the coding sequences encode enzymes that catalyze different parts of a synthetic pathway to form a desired product. In a genetic pathway, a first encoded enzyme uses a substrate to make a first product which in turn is used as a substrate for a second encoded enzyme to make a second product. In some embodiments, the genetic pathway includes 3 or more members (e.g., 3, 4, 5, 6, 7, 8, 9, etc.), wherein the product of one encoded enzyme is the substrate for the next enzyme in the synthetic pathway. As used herein, the term “genetically modified” denotes a host cell that contains a heterologous nucleotide sequence. The genetically modified host cells described herein typically do not exist in nature. As used herein, the term “heterologous” refers to what is not normally found in nature. The term “heterologous nucleic acid” refers to a nucleic acid not normally found in a given cell in nature. A heterologous nucleic acid can be: (a) foreign to its host cell, i.e., exogenous to the host cell such that a host cell does not naturally contain the nucleic acid; (b) naturally found in the host cell, i.e., endogenous or native to the host cell, but present at an unnatural quantity in the cell (i.e., greater or lesser quantity than naturally found in the host cell); (c) be naturally found in the host cell but positioned outside of its ATTORNEY DOCKET: 51494-029WO2 PATENT natural locus. A “heterologous” polypeptide refers to a polypeptide that is encoded by a “heterologous nucleic acid”. Thus, for example, a “heterologous” polypeptide may be naturally produced by a host cell but is encoded by a heterologous nucleic acid that has been introduced into the host cell by genetic engineering. For example, a “heterologous” polypeptide can include embodiments in which an endogenous polypeptide is produced by an expression construct and is overexpressed in the host cell compared to native levels of the polypeptide produced by the host cell. A “heterologous genetic pathway” or a “heterologous biosynthetic pathway” as used herein refer to a genetic pathway that does not normally or naturally exist in an organism or cell. The term “host cell” as used in the context of this disclosure refers to a microorganism, such as yeast, and includes an individual cell or cell culture including a heterologous vector or heterologous polynucleotide as described herein. Host cells include progeny of a single host cell, and the progeny may not necessarily be completely identical (in morphology or in total DNA complement) to the original parent cell due to natural, accidental, or deliberate mutation and/or change. A host cell includes cells into which a recombinant vector or a heterologous polynucleotide of the invention has been introduced, including by transformation, transfection, and the like. The terms “human milk oligosaccharide” and “HMO” are used interchangeably herein to refer to a group of nearly 200 identified sugar molecules that are found as the third most abundant component in human breast milk. HMOs in human breast milk are a complex mixture of free, indigestible carbohydrates with many different biological roles, including promoting the development of a functional infant immune system. HMOs include, without limitation, lacto-N-neotetraose (LNnT), 2’-fucosyllactose (2’-FL), 3- fucosyllactose (3-FL), difucosyllactose (DFL), lacto-N-tetraose (LNT), lacto-N-fucopentaose (LNFP) I, LNFP II, LNFP III, LNFP V, LNFP VI, lacto-N-difucohexaose (LNDFH) I, LNDFH II, lacto-N-hexaose (LNH), lacto-N-neohexaose (LNnH), fucosyllacto-N-hexaose (F-LNH) I, F-LNH II, difucosyllacto-N- hexaose (DFLNH) I, DFLNH II, difucosyllacto-N-neohexaose (DFLNnH), difucosyl-para-lacto-N-hexaose (DF-para-LNH), difucosyl-para-lacto-N-neohexaose (DF-para-LNnH), trifucosyllacto-N-hexaose (TF- LNH), 3’-siallylactose (3’-SL), 6’-siallylactose (6’-SL), sialyllacto-N-tetraose (LST) a, LST b, LST c, disialyllacto-N-tetraose (DS-LNT), fucosyl-sialyllacto-N-tetraose (F-LST) a, F-LST b, fucosyl-sialyllacto-N- hexaose (FS-LNH), fucosyl-sialyllacto-N-neohexaose (FS-LNnH) I, and fucosyl-disialyllacto-N-hexaose (FDS-LNH II), among others. As used herein, the term “medium” refers to culture medium and/or fermentation medium. The terms “modified,” “recombinant” and “engineered,” when used to modify a host cell described herein, refer to host cells or organisms that do not exist in nature, or express compounds, nucleic acids or proteins at levels that are not expressed by naturally occurring cells or organisms. As used herein, the phrase “operably linked” refers to a functional linkage between nucleic acid sequences such that the linked promoter and/or regulatory region functionally controls expression of the coding sequence. As used herein, the term “polyurethane” refers to a polymer which includes a chain including two or more monomer units which are joined together by carbamate linkages. As used herein, the term “production” generally refers to an amount of compound produced by a host cell provided herein. In some embodiments, production is expressed as a yield of the compound by ATTORNEY DOCKET: 51494-029WO2 PATENT the host cell. In other embodiments, production is expressed as a productivity of the host cell in producing the compound. As used herein, the term “steviol glycoside” refers to a glycoside of steviol including but not limited to 19-glycoside, steviolmonoside, steviolbioside, rubusoside, dulcoside B, dulcoside A, rebaudioside A (RebA), rebaudioside B (RebB), rebaudioside C (RebC), rebaudioside D (RebD), rebaudioside E (RebE), rebaudioside F (RebF), rebaudioside G (RebG), rebaudioside H (RebH), rebaudioside I (RebI), rebaudioside J (RebJ), rebaudioside K (RebK), rebaudioside L (RebL), rebaudioside M (RebM), rebaudioside N (RebN), rebaudioside O (RebO), rebaudioside D2, and rebaudioside M2. Brief Description of the Drawings FIG.1 is a graph characterizing the components of Farnesene Distillation Residue (FDR) obtained as a distillate residue from the fermentation of a population of β-farnesene-producing cells. FIG.2 shows a schematic of the process that was used to produce polyurethane films in Example 1, below. FIG.3 is an overlay of an FTIR spectrum of polyurethane films with the FTIR spectra of toluene diisocyanate (TDI), methylene diphenyl diisocyanate (MDI), hexamethylene diisocyanate (HDI), and isophorone diisocyanate (IPDI). FIG.4 is an overlay of x-ray diffraction diffractograms of bio-based polyurethanes obtained from Non-Distillate 1 (ND1) as described in Example 1 and different isocyanates. Detailed Description The present disclosure provides compositions and methods for synthesizing a polyurethane from a fermentation composition. The polyurethane may be synthesized, for example, by culturing a population of host cells capable of producing a fermentation product in a culture medium and under conditions suitable for the host cells to produce the fermentation product. The composition resulting from this fermentation process may include one or more polyols, which may be used in the synthesis of a polyurethane. However, isolating and refining these polyols in a way that prepares them for subsequent polymerization has been a long-standing challenge, particularly, because such are present in the fermentation composition along with impurities, including sludge and wax. These impurities have hindered the ability of such polyols to be utilized as starting materials for biopolymer production. It has presently been discovered that residue (e.g., a distillate residue) from a fermentation composition may be subjected to a unique series of steps in order to efficiently isolate and purify such polyols, rendering them capable of polymerization. For example, by purifying the residue (e.g., distillate residue) from a fermentation composition by way of a tandem extraction-distillation procedure, a polyol product may be obtained. The resulting polyol product may be reacted with an isocyanate to form polyurethane. The sections that follow provide a description of exemplary compositions and methods that may be used to synthesize a polyurethane from secondary materials produced during a fermentation process. ATTORNEY DOCKET: 51494-029WO2 PATENT Methods of Synthesizing a Polyurethane Provided herein are methods for synthesizing a polyurethane from a fermentation composition that has been produced by culturing a population of host cells capable of producing a fermentation product. For example, the production methods of the disclosure may include extracting an oil fraction from a residue (e.g., distillate residue) from the fermentation composition, distilling the oil fraction to produce a distillation product, and reacting the distillation product with an isocyanate to form the polyurethane. The extraction of an oil fraction from a distillate from the fermentation composition may include a winterization step. The winterization step may include dissolving the distillate from the fermentation composition in ethanol to produce an ethanol solution. The ratio of the residue (e.g., distillate residue) from the fermentation composition to ethanol may be between 1:8 (w/v) and 1:1 (w/v) (e.g., between 1:7 (w/v) and 1:1 (w/v), 1:6 (w/v) and 1:1 (w/v), 1:5 (w/v) and 1:1 (w/v), 1:4 (w/v) and 1:1 (w/v), 1:3 (w/v) and 1:1 (w/v), 1:2 (w/v) and 1:1 (w/v), 1:8 (w/v) and 1:2 (w/v), 1:8 (w/v) and 1:3 (w/v), 1:8 (w/v) and 1:4 (w/v), 1:8 (w/v) and 1:5 (w/v), 1:8 (w/v) and 1:6 (w/v), or 1:8 (w/v) and 1:7 (w/v). For example, the residue (e.g., distillate residue) from the fermentation composition and the ethanol may have a ratio of 1:8 (w/v), 1:7 (w/v), 1:6 (w/v), 1:5 (w/v), 1:4 (w/v), 1:3 (w/v), or 1:2 (w/v). In some embodiments, the residue (e.g., distillate residue) from the fermentation composition and the ethanol are present in a ratio of 1:4 (w/v). The distillate from the fermentation composition and the ethanol may be mixed for between about 1 minute and about 1 hour (e.g., between about 10 minutes and 1 hour, 20 minutes and 1 hour, 30 minutes and 1 hour, 40 minutes and 1 hour, 50 minutes and 1 hour, 1 minute and 50 minutes, 1 minute and 40 minutes, 1 minute and 30 minutes, 1 minute and 20 minutes, or 1 minute and 10 minutes). For example, the distillate from the fermentation composition and the ethanol may be mixed for between about 1 minute and about 20 minutes (e.g., 1 minute, 2 minutes, 3 minutes, 4 minutes, 5 minutes, 6 minutes, 7 minutes, 8 minutes, 9 minutes, 10 minutes, 11 minutes, 12 minutes, 13 minutes, 14 minutes, 15 minutes, 16 minutes, 17 minutes, 18 minutes, 19 minutes, or 20 minutes). In some embodiments, the residue (e.g., distillate residue) from the fermentation composition and the ethanol are mixed for about 5 minutes. The ethanol solution may be left to stand after being mixed for between about 10 minutes and about 6 hours (e.g., between about 10 minutes and 5 hours, 10 minutes and 4 hours, 10 minutes and 3 hours, 10 minutes and 2 hours, 10 minutes and 1 hour, 1 hour and 6 hours, 2 hours and 6 hours, 3 hours and 6 hours, 4 hours and 6 hours, or 5 hours and 6 hours). For example, the ethanol solution may be left to stand for between about 1 hour and about 3 hours (e.g., between about 60 minutes and about 90 minutes, about 60 minutes and about 2 hours, about 60 minutes and about 150 minutes, or about 60 minutes and about 2 hours). In some embodiments, the ethanol solution is let stand for about 2 hours. The ethanol solution may be left to stand at room temperature. After the ethanol solution is let stand, the ethanol solution may be chilled. The ethanol solution may be chilled at a temperature of between about -50 ^o C and about 0 ^o C, such as between about -40 ^o C and 0 ^o C, -30 ^o C and 0 ^o C, -20 ^o C and 0 ^o C, -10 ^o C and 0 ^o C, and -30 ^o C and -10 ^o C. In some embodiments, the ethanol solution may be chilled to a temperature of between about -40 ^o C and about - 20 ^o C; for example, about -40 ^o C, -35 ^o C, -30 ^o C, -25 ^o C, or -20 ^o C. The ethanol solution may be chilled to about -30 ^o C. The ethanol solution may be chilled for a period of time. In some embodiments, the ethanol solution is chilled for anywhere between 1 hour and 24 hours; for example, it may be chilled for ATTORNEY DOCKET: 51494-029WO2 PATENT between 1 hour and 18 hours, 1 hour and 12 hours, 1 hour and 6 hours, 6 hours and 24 hours, 12 hours and 24 hours, 18 hours and 24 hours, or 6 hours and 18 hours. The ethanol solution may be chilled for between 8 hours and 16 hours (e.g., 8 hours, 9 hours, 10 hours, 11 hours, 12 hours, 13 hours, 14 hours, 15 hours, or 16 hours. The winterization step may also include a centrifugation step, where the ethanol solution is centrifuged. The centrifugation of the ethanol solution may be performed at a speed of between about 500 g and about 2000 g (e.g., between about 500 g and 1500 g, 500 g and 1000 g, 1000 g, and 2000 g, 1500 g and 2000 g, or 1000 g and 1500 g). For example, the centrifugation may be performed at a speed of between about 1000 g and about 1500 g (e.g., between about 1000 g and 1400 g, 1000 g and 1300 g, 1000 g and 1200 g, 1000 g and 1100 g, 1100 g and 1500 g, 1200 g and 1500 g, 1300 g and 1500 g, or 1400 g and 1500 g). In some embodiments, the centrifugation of the ethanol solution is performed at a speed of about 1250 g. The centrifugation of the ethanol solution may be performed at room temperature. Furthermore, the centrifugation may occur for between about 1 minute and about 30 minutes. The extraction of the oil from the residue (e.g., distillate residue) from the fermentation composition may include a filtration step. In some embodiments, the extraction of the oil from the residue (e.g., distillate residue) from the fermentation composition may include one or more filtration steps. In some embodiments, the filtration includes at least two filtration steps. For example, the extraction of the oil from the residue (e.g., distillate residue) from the fermentation composition may include one, two, three, four, five, or more filtration steps. The extraction of the oil from the residue (e.g., distillate residue) from the fermentation composition may include a first filtration step, a second filtration step, and a third filtration step. The first filtration step may include filtering the residue (e.g., distillate residue) from a fermentation composition through a nonwoven (TNT) filter. The second filtration step may include filtering the filtrate from the first filtration step though a membrane that is between 5 µm and 15 µm in pore size; for example, the membrane may be about 5 µm, 6 µm, 7 µm, 8 µm, 9 µm, 10 µm, 11 µm, 12 µm, 13 µm, 14 µm, or 15 µm in pore size. In some embodiments, the membrane is 11 µm in pore size. The third filtration step may include filtering the filtrate of the second filtration step through a filter having a membrane that is between 5 µm and 15 µm in pore size; for example, the membrane may be about 5 µm, 6 µm, 7 µm, 8 µm, 9 µm, 10 µm, 11 µm, 12 µm, 13 µm, 14 µm, or 15 µm in pore size. In some embodiments, the membrane has a filter that is about 8 µm in pore size. One or more the filtration steps may be performed under vacuum. The extraction of the oil from the residue (e.g., distillate residue) from the fermentation composition may include a winterization step and one or more filtration steps. The method also includes a distillation step wherein the oil fraction obtained by extraction of the residue (e.g., distillate residue) from the fermentation composition to produce a distillation product. The distillation step may include short path distillation. The distillation may be performed at a temperature of between about 125 ^o C and about 250 ^o C; for example, the temperature may be between 150 ^o C and 250 ^o C, 175 ^o C and 250 ^o C, 200 ^o C and 250 ^o C, 225 ^o C and 250 ^o C, 125 ^o C and 225 ^o C, 125 ^o C and 200 ^o C, 125 ^o C and 175 ^o C, or 125 ^o C and 150 ^o C. In some embodiments, the distillation step may be performed at a temperature of between 170 ^o C and 190 ^o C (e.g., 170 ^o C, 175 ^o C, 180 ^o C, 185 ^o C, or 190 ^o C). In some embodiments, the distillation step may be performed at a temperature of about 180 ^o C. ATTORNEY DOCKET: 51494-029WO2 PATENT The distillation step may be performed at a pressure of between about 0.01 mbar and about 1 mbar (e.g., between about 0.01 mbar and about 0.75 mbar, about 0.01 mbar and about 0.5 mbar about 0.01 mbar and about 0.25 mbar, about 0.01 mbar and about 0.1 mbar, about 0.01 mbar and about 0.05 mbar, about 0.05 mbar and about 1 mbar, about 0.1 mbar and about 1 mbar, about 0.25 mbar and about 1 mbar, about 0.5 mbar and about 1 mbar, or about 0.75 mbar and about 1 mbar). For example, the distillation step may be performed at a pressure of between about 0.05 mbar and about 0.5 mbar (e.g., between about 0.05 mbar and about 0.4 mbar, about 0.05 mbar and about 0.3 mbar, about 0.05 mbar and about 0.2 mbar, about 0.05 mbar and about 0.1 mbar, about 0.1 mbar and about 0.5 mbar, about 0.2 mbar and about 0.5 mbar, about 0.3 mbar and about 0.5 mbar, or about 0.4 mbar and about 0.5 mbar). In some embodiments, the distillation step may be performed at a pressure of about 0.1 mbar. The distillation step may be performed at a feed rat of between about 0.5 mL/min and about 2.5 mL/min (e.g., between about 1 mL/min and about 2.5 mL/min, about 1.5 mL/min and about 2.5 mL/min, about 2 mL/min and about 2.5 mL/min, about 0.5 mL/min and about 2 mL/min, about 1 mL/min and about 2 mL/min, or about 1.5 mL/min and about 2 mL/min). For example, the distillation step is performed at a feed rate of between about 1 mL/min and about 2 mL/min (e.g., about 1.1 mL/min, 1.2 mL/min, 1.3 mL/min, 1.4 mL/min, 1.5 mL/min, 1.6 mL/min, 1.7 mL/min, 1.8 mL/min, 1.9 mL/min, or 2 mL/min). In some embodiments, distillation step is performed at a feed rate of about 1.5 mL/min. The distillation step may be performed using rotation. The distillation step may be performed at a rotor rate of between about 100 rpm and about 500 rpm (e.g., between about 100 rpm and about 400 rpm, about 100 rpm and about 300 rpm, about 100 rpm and about 200 rpm, about 200 rpm and about 500 rpm, about 300 rpm and about 500 rpm, or about 400 rpm and about 500 rpm). Furthermore, the method includes a reacting the distillation product with an isocyanate to form the polyurethane. The distillation product and the isocyanate may be reacted in a ratio of between about 5:1 (w/w) and about 1:5 (w/w) (e.g., about 3:1 (w/w) and about 1:5 (w/w), about 1:1 (w/w) and about 1:5 (w/w), about 1:2 (w/w) and about 1:5 (w/w), about 5:1 (w/w) and about 1:2 (w/w), about 5:1 (w/w) and about 1:1 (w/w), about 5:1 (w/w) and about 2:1(w/w), or about 5:1 (w/w) and about 4:1 (w/w)). For example, the distillation product and the isocyanate may be reacted in a ratio of between about 3:1 (w/w) and about 1:1 (w/w) (e.g., about 3:1 (w/w), about 2:1 (w/w), or about 1:1 (w/w)). In some embodiments, the distillation product and the isocyanate are reacted in a ratio of about 7:3 (w/w). The isocyanate may be any isocyanate; for example, the isocyanate may include one or more of toluene diisocyanate (TDI), methylenediphenyl diisocyanate (MDI), hexamethylene diisocyanate (HDI), or isophorone diisocyanate (IPDI). In some embodiments, the isocyanate used is TDI. In some embodiments, the isocyanate used is MDI. In some embodiments, the isocyanate used is IPDI. In some embodiments, the isocyanate used is HDI. The reacting step may further includes contacting the distillation product of with venyltimethoxy silane. The vinyltrimethyoxy silane may be present in a final concentration of between about 1% (w/v) and about 3 % (w/v). For example, the vinyltrimethyoxy silane may have a concentration of between about 1% (w/v) and about 2.5% (w/v), about 1% (w/v) and 2% (w/v), about 1% (w/v) and 1.5% (w/v), about 1.5% (w/v) and 3% (w/v), about 2% (w/v) and 3% (w/v), or about 2.5% (w/v) and 3% (w/v). In some embodiments, the vinyltrimethoxy silane has a final concentration of about 2% (w/v). ATTORNEY DOCKET: 51494-029WO2 PATENT The reacting step may further include contacting the distillation product) with a catalyst. The catalyst may be present in a final concentration of between about 0.05% (w/v) and about 1% (w/v) (e.g., about 0.1% (w/v) and about 1% (w/v), about 0.5% (w/v) and about 1, about 0.75% (w/v) and about 1% (w/v), 0.05% (w/v) and about 0.75% (w/v), about 0.05% (w/v) and about 0.5% (w/v), or about 0.05% (w/v) and about 0.1% (w/v)). In some embodiments, the catalyst is present in a final concentration of between about 0.1% (w/v) and about 0.5% (w/v) (e.g., about 0.1% (w/v), about 0.2% (w/v), about 0.3% (w/v), about 0.4% (w/v), or about 0.5% (w/v)). For example, the catalyst is present in a final concentration of 0.2% (w/v). The catalyst may be dibutyltin dilaurate. The reacting of the distillation product with the isocyanate may be performed at a temperature of between about 25 ^o C and about 100 ^o C (e.g., between about 25 ^o C and about 75 ^o C, about 25 ^o C and about 50 ^o C, about 50 ^o C and about 100 ^o C, or about 75 ^o C and about 100 ^o C). For example, the reacting step is performed at a temperature of between about 50 ^o C and about 90 ^o C (e.g., between about 50 ^o C and about 80 ^o C, about 50 ^o C and about 70 ^o C, about 50 ^o C and about 60 ^o C, about 60 ^o C and about 90 ^o C, about 70 ^o C and about 90 ^o C, or 80 ^o C and about 90 ^o C). In some embodiments, the reacting step is performed at a temperature of about 70 ^o C. The reacting of the distillation product with the isocyanate may be performed for between about 12 hours and about 72 hours (e.g., between about 12 hours and about 60 hours, about 12 hours and about 48 hours, about 12 hours and about 36 hours, about 12 hours and about 24 hours, about 24 hours and about 72 hours, about 36 hours and about 72 hours, about 48 hours and about 72 hours, or about 60 hours and about 72 hours). In some embodiments, the reacting of the distillation product with the isocyanate is performed for between about 36 hours and about 60 hours (e.g., between about 42 hours and about 60 hours, about 48 hours and about 60 hours, about 54 hours and about 60 hours, about 36 hours and about 54 hours, about 36 hours and about 48 hours, or about 36 hours and about 42 hours). For example, the reacting of the distillation product with the isocyanate is performed for about 48 hours. The polyurethane synthesized using any one of the methods described herein may be characterized with respect to its Young modulus or by how much it may be elongated before it breaks. The polyurethane may have an elongation at break of between about 20% and about 1000% (e.g., between about 20% and about 800%, about 20% and about 600%, about 20% and about 400%, about 20% and about 200%, about 20% and about 50%, about 50% and about 1000%, about 200% and about 1000%, about 400% and about 1000%, about 600% and about 1000%, or about 800% and about 1000%). For example, the polyurethane may have an elongation at break of between about 50% and about 700% (e.g., about 50% and about 600%, about 50% and about 500%, about 50% and about 400%, about 50% and about 300%, about 50% and about 200%, about 50% and about 100%, about 100% and about 700%, about 200% and about 700%, about 300% and about 700%, about 400% and about 700%, about 500% and about 700%, or about 600% and about 700%). The polyurethane which has been synthesized may have a Young modulus of between about 0.1 MPa and about 4 MPa (e.g., between about 0.1 MPa and about 3 MPa, about 0.1 MPa and about 2 MPa, about 0.1 MPa and about 1 MPa, about 0.1 MPa and about 0.5 MPa, about 0.5 MPa and about 4 MPa, about 1 MPa and about 4 MPa, about 2 MPa and about 4 MPa, or about 3 MPa and about 4 MPa). For example, the polyurethane may have a Young modulus of between about 0.2 MPa and about 3.5 MPa (e.g., between about 0.2 MPa and about 3 MPa, about 0.2 MPa and about 2.5 MPa, about 0.2 MPa and about 2 MPa, about 0.2 MPa and ATTORNEY DOCKET: 51494-029WO2 PATENT about 1.5 MPa, about 0.2 MPa and about 1 MPa, about 0.2 MPa and about 0.5 MPa, about 0.5 MPa and about 3.5 MPa, about 1 MPa and about 3.5 MPa, about 1.5 MPa and about 3.5 MPa, about 2 MPa and about 3.5 MPa, about 2.5 MPa and about 3.5 MPa, or about 3 MPa and about 3.5 MPa). Enzymes of Exemplary Biosynthetic Pathways The host cells described herein may express one or more enzymes of a biosynthetic pathway capable of producing a fermentation product of interest. In some embodiments, for example, host cells and/or previously fermented cells of the disclosure (e.g., yeast cells) may naturally express some of the enzymes of the biosynthetic pathway for a given fermentation product. Such cells may be modified to express the remaining or heterologous enzymes of the biosynthetic pathway. In some embodiments, for instance, a cell (e.g., a yeast cell) may naturally express many of the enzymes of the biosynthetic pathway of a desired fermentation product, and the cells may be modified so as to express the remaining enzymes of the biosynthetic pathway for the desired fermentation product by providing the cells with one or more heterologous nucleic acid molecules that, together, encode the remaining enzymes of the biosynthetic pathway. In some embodiments, the cells may be genetically modified to produce a fermentation product. The cells may produce a fermentation product such as, for example, an isoprene, an isoprenoid, β-farnesene, a human milk oligosaccharide (HMO), a steviol glycoside, or a cannabinoid. Isoprenoid Biosynthetic Pathway The cells described herein may be modified to express one or more enzymes of the mevalonate- dependent (MEV) biosynthetic pathway. Cells which are modified with one or more enzymes of the MEV biosynthetic pathway may be capable of an increased production of one or more isoprenoid compounds as compared to cell which is not modified with one or enzymes of the MEV biosynthetic pathway. In some embodiments, the isoprenoid producing cell comprises a heterologous nucleotide sequence encoding an enzyme that can condense two molecules of acetyl-coenzyme A to form acetoacetyl-CoA, e.g., an acetyl-CoA thiolase. Illustrative examples of nucleotide sequences encoding such an enzyme include but are not limited to: (NC_000913 REGION: 2324131.2325315; Escherichia coli), (D49362; Paracoccus denitrifzcans), and (L20428; Saccharomyces cerevisiae). In some embodiments, the cell includes a heterologous nucleotide sequence encoding an enzyme that can condense acetoacetyl-CoA with another molecule of acetyl-CoA to form 3-hydroxy-3- methylglutaryl-CoA (HMG-CoA), e.g., a HMGCoA synthase. Illustrative examples of nucleotide sequences encoding such an enzyme include but are not limited to: (NC_00l 145. complement 19061.20536; Saccharomyces cerevisiae), (X96617; Saccharomyces cerevisiae), (X83882; Arabidopsis thaliana), (AB037907; Kitasatospora griseola), (BT007302; Homo sapiens), and (NC_002758, Locus tag SAV2546, GeneID 1122571; Staphylococcus aureus). In some embodiments, the cell includes a heterologous nucleotide sequence encoding an enzyme that can convert HMG-CoA into mevalonate, e.g., an HMG-CoA reductase. Illustrative examples of nucleotide sequences encoding such an enzyme include, but are not limited to: (NM_206548; Drosophila melanogaster), (NC_002758, Locus tag SAV2545, GeneID 1122570; Staphylococcus aureus), (NM_204485; Gallus gallus), (AB015627; Streptomyces sp. KO 3988), (AF542543; Nicotiana attenuata), (AB037907; Kitasatospora griseola), (AX128213, providing the sequence encoding a truncated HMGR; ATTORNEY DOCKET: 51494-029WO2 PATENT Saccharomyces cerevisiae), and (NC_001145: complement (115734.118898; Saccharomyces cerevisiae). In some embodiments, the cells include a heterologous nucleotide sequence encoding an enzyme that can convert mevalonate into mevalonate 5-phosphate, e.g., a mevalonate kinase. Illustrative examples of nucleotide sequences encoding such an enzyme include but are not limited to: (L77688; Arabidopsis thaliana), and (X55875; Saccharomyces cerevisiae). In some embodiments, the cells include a heterologous nucleotide sequence encoding an enzyme that can convert mevalonate 5-phosphate into mevalonate 5-pyrophosphate, e.g., a phosphomevalonate kinase. Illustrative examples of nucleotide sequences encoding such an enzyme include but are not limited to: (Af 429385; Hevea brasiliensis), (NM_006556; Homo sapiens), and (NC_00l 145. Complement 712315.713670; Saccharomyces cerevisiae). In some embodiments, the cells include a heterologous nucleotide sequence encoding an enzyme that can convert mevalonate 5-pyrophosphate into isopentenyl diphosphate (IPP), e.g., a mevalonate pyrophosphate decarboxylase. Illustrative examples of nucleotide sequences encoding such an enzyme include but are not limited to: (X97557; Saccharomyces cerevisiae), (AF290095; Enterococcus faecium), and (U49260; Homo sapiens). In some embodiments, the cells include one or more heterologous nucleotide sequences encoding more than one enzyme of the MEV pathway. In some embodiments, the cell includes one or more heterologous nucleotide sequences encoding two enzymes of the MEV pathway. In some embodiments, the cell includes one or more heterologous nucleotide sequences encoding an enzyme that can convert HMG-CoA into mevalonate and an enzyme that can convert mevalonate into mevalonate 5-phosphate. In some embodiments, the cell includes one or more heterologous nucleotide sequences encoding three enzymes of the MEV pathway. In some embodiments, the cell includes one or more heterologous nucleotide sequences encoding four enzymes of the MEV pathway. In some embodiments, the cell includes one or more heterologous nucleotide sequences encoding five enzymes of the MEV pathway. In some embodiments, the cell includes one or more heterologous nucleotide sequences encoding six enzymes of the MEV pathway. In some embodiments, the cell further includes a heterologous nucleotide sequence encoding an enzyme that can convert IPP generated via the MEV pathway into its isomer, dimethylallyl pyrophosphate (DMAPP). DMAPP can be condensed and modified through the action of various additional enzymes to form simple and more complex isoprenoids. The cells described herein may be modified to express one or more enzymes of the 1-deoxy-D- xylulose 5-diphosphate (DXP) biosynthetic pathway. Cells which are modified with one or more enzymes of the DXP biosynthetic pathway may be capable of an increased production of one or more isoprenoid compounds as compared to cell which is not modified with one or enzymes of the DXP biosynthetic pathway. In some embodiments, the cells include a heterologous nucleotide sequence encoding an enzyme that can condense two molecules of acetyl-coenzyme A to form acetoacetyl-CoA, e.g., an acetyl- CoA thiolase. Illustrative examples of nucleotide sequences encoding such an enzyme include but are not limited to: (NC_000913 REGION: 2324131.2325315; Escherichia coli), (D49362; Paracoccus denitrifzcans), and (L20428; Saccharomyces cerevisiae). ATTORNEY DOCKET: 51494-029WO2 PATENT In some embodiments, the cell includes a heterologous nucleotide sequence encoding an enzyme, e.g., l-deoxy-D-xylulose-5-phosphate synthase, which can condense pyruvate with D- glyceraldehyde 3-phosphate to make l-deoxy-D-xylulose- 5-phosphate. Illustrative examples of nucleotide sequences encoding such an enzyme include but are not limited to: (AF035440; Escherichia coli), (NC_002947, locus tag PP0527; Pseudomonas putida KT2440), (CP000026, locus tag SPA2301; Salmonella enterica Paratyphi, see ATCC 9150), (NC_007493, locus tag RSP _0254; Rhodobacter sphaeroides 2.4.1 ), (NC_ 005296, locus tag RP A0952; Rhodopseudomonas palustris CGA009), (NC_004556, locus tag PD1293; Xylellafastidiosa Temecula]), and (NC_003076, locus tag AT5Gl 1380; Arabidopsis thaliana). In some embodiments, the cell includes a heterologous nucleotide sequence encoding an enzyme, e.g., l-deoxy-D-xylulose-5-phosphate reductoisomerase, which can convert l-deoxy-D-xylulose- 5-phosphate to 2C-methyl-Derythritol- 4-phosphate. Illustrative examples of nucleotide sequences include but are not limited to: (AB013300; Escherichia coli), (AF148852; Arabidopsis thaliana), (NC_002947, locus tag PP1597; Pseudomonas putida KT2440), (AL939124, locus tag SCO5694; Streptomyces coelicolor A3(2)), (NC_007493, locus tag RSP 2709; Rhodobacter sphaeroides 2.4.1), and (NC_007492, locus tag Pfl_l 107; Pseudomonas jluorescens PfO-1). In some embodiments, the cell includes a heterologous nucleotide sequence encoding an enzyme, e.g., 4-diphosphocytidyl-2C-methyl-D-erythritol synthase, which can convert 2C-methyl-D- erythritol-4-phosphate to 4-diphosphocytidyl-2Cmethyl-D-erythritol. Illustrative examples of nucleotide sequences include but are not limited to: (AF230736; Escherichia coli), (NC_007493, locus tag RSP 2835; Rhodobacter sphaeroides 2.4.1), (NC_003071, locus tag AT2G02500; Arabidopsis thaliana), and (NC_002947, locus tag PP1614; Pseudomonas putida KT2440). In some embodiments, the cell includes a heterologous nucleotide sequence encoding an enzyme, e.g., 4-diphosphocytidyl-2C-methyl-D-erythritol kinase, which can convert 4-diphosphocytidyl- 2C-methyl-D-erythritol to 4-diphosphocytidyl-2C-methyl-D-erythritol-2-phosphate. Illustrative examples of nucleotide sequences include but are not limited to: (AF216300; Escherichia coli) and (NC_007493, locus tag RSP 1779; Rhodobacter sphaeroides 2.4.1). In some embodiments, the cell includes a heterologous nucleotide sequence encoding an enzyme, 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase, which can convert 4-diphosphocytidyl- 2C-methyl-D-erythritol-2-phosphate to 2Cmethyl-D-erythritol 2,4-cyclodiphosphate. Illustrative examples of nucleotide sequences include but are not limited to: (AF230738; Escherichia coli), (NC_007493, locus tag RSP _6071; Rhodobacter sphaeroides 2.4.1), and (NC_002947, locus tag PP1618; Pseudomonas putida KT2440). In some embodiments, the cell includes a heterologous nucleotide sequence encoding an enzyme, e.g., l-hydroxy-2-methyl-2-(E)-butenyl-4- diphosphate synthase, which can convert 2C-methyl-D- erythritol 2,4-cyclodiphosphate to 1- hydroxy-2-methy 1-2-(E)-butenyl 1-4-di phosphate. Illustrative examples of nucleotide sequences include but are not limited to: (AY033515; Escherichia coli), (NC_002947, locus tag PP0853; Pseudomonas putida KT2440), and (NC_007493, locus tag RSP 2982; Rhodobacter sphaeroides 2.4.1). In some embodiments, the cell includes a heterologous nucleotide sequence encoding an enzyme, e.g., isopentyl/dimethylallyl diphosphate synthase, which can convert l-hydroxy-2-methyl-2-(E)- ATTORNEY DOCKET: 51494-029WO2 PATENT butenyl-4-diphosphate into either IPP or its isomer, DMAPP. Illustrative examples of nucleotide sequences include but are not limited to: (AY062212; Escherichia coli) and (NC_002947, locus tag PP0606; Pseudomonas putida KT2440). In some embodiments, the cell includes one or more heterologous nucleotide sequences encoding more than one enzyme of the DXP pathway. In some embodiments, the cell includes one or more heterologous nucleotide sequences encoding two enzymes of the DXP pathway. In some embodiments, the cell includes one or more heterologous nucleotide sequences encoding three enzymes of the DXP pathway. In some embodiments, the cell includes one or more heterologous nucleotide sequences encoding four enzymes of the DXP pathway. In some embodiments, the cell includes one or more heterologous nucleotide sequences encoding five enzymes of the DXP pathway. In some embodiments, the cell includes one or more heterologous nucleotide sequences encoding six enzymes of the DXP pathway. In some embodiments, the cell includes one or more heterologous nucleotide sequences encoding five enzymes of the DXP pathway. In some embodiments, the cell includes one or more heterologous nucleotide sequences encoding seven enzymes of the DXP pathway. In some embodiments, "cross talk" (or interference) between the cell's own metabolic processes and those processes involved with the production of IPP are minimized or eliminated entirely. For example, cross talk is minimized or eliminated entirely when the cell relies exclusively on the DXP pathway for synthesizing IPP, and a MEV pathway is introduced to provide additional IPP. Such a cell would not be equipped to alter the expression of the MEV pathway enzymes or process the intermediates associated with the MEV pathway. Organisms that rely exclusively or predominately on the DXP pathway include, for example, Escherichia coli. In some embodiments, the cell produces IPP via the MEV pathway, either exclusively or in combination with the DXP pathway. In other embodiments, a cell’s DXP pathway is functionally disabled so that the cell produces IPP exclusively through a heterologously introduced MEV pathway. The DXP pathway can be functionally disabled by disabling gene expression or inactivating the function of one or more of the DXP pathway enzymes. In some embodiments, the cell further includes a heterologous nucleotide sequence encoding a polyprenyl synthase that can condense IPP and/or DMAPP molecules to form polyprenyl compounds containing more than five carbons. In some embodiments, the isoprenoid producing cell further comprises a heterologous nucleotide sequence encoding an enzyme that can convert IPP generated via the MEV pathway into DMAPP, e.g., an IPP isomerase. Illustrative examples of nucleotide sequences encoding such an enzyme include but are not limited to: (NC_000913, 3031087.3031635; Escherichia coli), and (AF082326; Haematococcus pluvialis). In some embodiments, the cell includes a heterologous nucleotide sequence encoding an enzyme that can condense one molecule of IPP with one molecule of DMAPP to form one molecule of geranyl pyrophosphate (GPP), e.g., a GPP synthase. Illustrative examples of nucleotide sequences encoding such an enzyme include, but are not limited to: (AF513lll;Abies grandis), (AF513112;Abies grandis), (AF513113;Abies grandis), (AY534686; Antirrhinum majus), (AY534687; Antirrhinum majus), (Yl 7376; Arabidopsis thaliana), (AE016877, Locus APl 1092; Bacillus cereus; ATCC 14579), (AJ243739; Citrus sinensis), (AY534745; Clarkia breweri), (AY953508; fps pini), (DQ286930; Lycopersicon ATTORNEY DOCKET: 51494-029WO2 PATENT esculentum), (AF182828; Mentha x piperita), (AF182827; Mentha x piperita), (MPI249453; Mentha x piperita), (PZE431697, Locus CAD24425; Paracoccus zeaxanthinifaciens), (A Y866498; Picrorhiza kurrooa), (A Y35 l 862; Vi tis vinifera), and (AF203881, Locus AAF12843; Zymomonas mobilis). In some embodiments, the cell includes a heterologous nucleotide sequence encoding an enzyme that can condense two molecules of IPP with one molecule of DMAPP or add a molecule of IPP to a molecule of GPP, to form a molecule of farnesyl pyrophosphate (FPP), e.g., a FPP synthase. Illustrative examples of nucleotide sequences that encode such an enzyme include, but are not limited to: (ATU80605; Arabidopsis thaliana), (ATHFPS2R; Arabidopsis thaliana), (AAU36376; Artemisia annua), (AF461050; Bos taurus), (D00694; Escherichia coli K-12), (AE009951, Locus AAL95523; Fusobacterium nucleatum subsp. nucleatum ATCC 25586), (GFFPPSGEN; Gibberella Jujikuroi), (CP000009, Locus AAW60034; Gluconobacter oxydans 621H), (AF019892; Helianthus annuus ), (HUMP APS; Homo sapiens), (KLPFPSQCR; Kluyveromyces lactis ), (LAU15777; Lupinus albus), (LAU20771; Lupinus albus), (AF309508; Mus musculus), (NCFPPSGEN; Neurospora crassa), (PAFPSl; Parthenium argentatum), (PAFPS2; Parthenium argentatum), (RA TF APS; Rattus norvegicus), (YSCFPP; Saccharomyces cerevisiae), (D89104; SchizoSaccharomyces pombe), (CP000003, Locus AAT87386; Streptococcus pyogenes), (CP0000l 7, Locus AAZ51849; Streptococcus pyogenes), (NC_ 008022, Locus YP 598856; Streptococcus pyogenes MGAS 10270), (NC_ 008023, Locus YP 600845; Streptococcus pyogenes MGAS2096), (NC_008024, Locus YP 602832; Streptococcus pyogenes MGAS10750), (MZEFPS; Zea mays), (AE000657, Locus AAC06913; Aquifex aeolicus VF5), (NM_202836; Arabidopsis thaliana), (D84432, Locus BAA12575; Bacillus subtilis), (Ul2678, Locus AAC28894; Bradyrhizobiumjaponicum USDA 110), (BACFDPS; Geobacillus stearothermophilus), (NC_002940, Locus NP 873754; Haemophilus ducreyi 35000HP), (L42023, Locus AAC23087; Haemophilus injluenzae Rd KW20), (J05262; Homo sapiens), (YP 395294; Lactobacillus sakei subsp. sakei 23K), (NC_005823, Locus YP 000273; Leptospira interrogans serovar Copenhageni str. Fiocruz Ll-130), (AB003187; Micrococcus luteus), (NC_002946, Locus YP _208768; Neisseria gonorrhoeae FA 1090), (U00090, Locus AAB91752; Rhizobium sp. NGR234), (J05091; Saccharomyces cerevisiae), (CP000031, Locus AAV93568; Silicibacter pomeroyi DSS-3), (AE008481, Locus AAK99890; Streptococcus pneumoniae R6), and (NC_ 004556, Locus NP 779706; Xylella fastidiosa Temecula1). In some embodiments, the cell includes a heterologous nucleotide sequence encoding an enzyme that can combine IPP and DMAPP or IPP and FPP to form geranylgeranyl pyrophosphate (GGPP). Illustrative examples of nucleotide sequences that encode such an enzyme include, but are not limited to: (ATHGERPYRS; Arabidopsis thaliana), (BT005328; Arabidopsis thaliana), (NM_l 19845; Arabidopsis thaliana), (NZ_AAJM01000380, Locus ZP 00743052; Bacillus thuringiensis serovar israelensis, ATCC 35646 sql563), (CRGGPPS; Catharanthus roseus), (NZ_AABF02000074, Locus ZP 00144509; Fusobacterium nucleatum subsp. vincentii, ATCC 49256), (GFGGPPSGN; Gibberellafujikuroi), (AY371321; Ginkgo biloba), (AB055496; Hevea brasiliensis), (AB0l 7971; Homo sapiens), (MCI276129; Mucor circinelloides f. lusitanicus), (AB016044; Mus musculus), (AABX01000298, Locus NCU01427; Neurospora crassa), (NCU20940; Neurospora crassa), (NZ_AAKL01000008, Locus ZP 00943566; Ralstonia solanacearum UW551), (ABl 18238; Rattus norvegicus), (SCU31632; Saccharomyces cerevisiae), (AB016095; Synechococcus elongates), (SAGGPS; Sinapis alba), (SSOGDS; Sulfolobus acidocaldarius), (NC_007759, Locus YP 461832; Syntrophus aciditrophicus SB), ATTORNEY DOCKET: 51494-029WO2 PATENT (NC_006840, Locus YP 204095; Vibrio jischeri ESl 14), (NM_ 112315; Arabidopsis thaliana), (ERWCR TE; Pantoea agglomerans), (D90087, Locus BAA14124; Pantoea ananatis), (X52291, Locus CAA36538; Rhodobacter capsulatus), (AF195122, Locus AAF24294; Rhodobacter sphaeroides), and (NC_004350, Locus NP 721015; Streptococcus mutans UA159). In some embodiments, the cell further includes a heterologous nucleotide sequence encoding an enzyme that can modify a polyprenyl to form a hemiterpene, a monoterpene, a sesquiterpene, a diterpene, a triterpene, a tetraterpene, a polyterpene, a steroid compound, a carotenoid, or a modified isoprenoid compound. In some embodiments, the heterologous nucleotide encodes a carene synthase. Illustrative examples of suitable nucleotide sequences include, but are not limited to: (AF461460, REGION 43.1926; Picea abies) and (AF527416, REGION: 78.1871; Salvia stenophylla). In some embodiments, the heterologous nucleotide encodes a geraniol synthase. Illustrative examples of suitable nucleotide sequences include but are not limited to: (Af 457070; Cinnamomum tenuipilum), (A Y362553; Ocimum basilicum), (DQ234300; Perilla frutescens strain 1864), (DQ234299; Perilla citriodora strain 1861), (DQ234298; Perilla citriodora strain 4935), and (DQ088667; Perilla citriodora). In some embodiments, the heterologous nucleotide encodes a linalool synthase. Illustrative examples of a suitable nucleotide sequence include, but are not limited to: (AF497485; Arabidopsis thaliana), (AC002294, Locus AAB71482; Arabidopsis thaliana), (AY059757; Arabidopsis thaliana), (NM_104793; Arabidopsis thaliana), (AF154124; Artemisia annua), (AF067603; Clarkia breweri), (AF067602; Clarkia concinna), (AF067601; Clarkia breweri), (U58314; Clarkia breweri), (AY840091; Lycopersicon esculentum), (DQ263741; Lavandula angustifolia), (AY083653;Mentha citrate), (AY693647; Ocimum basilicum), (XM_ 463918; Oryza sativa), (AP004078, Locus BAD07605; Oryza sativa), (XM_ 463918, Locus XP _ 463918; Oryza sativa), (AY917193; Perilla citriodora), (AF271259; Perillafrutescens), (AY473623; Picea abies), (DQ195274; Picea sitchensis), and (AF444798; Perilla frutescens var. crispa cultivar No.79). In some embodiments, the heterologous nucleotide encodes a limonene synthase. Illustrative examples of suitable nucleotide sequences include but are not limited to:(+) limonene synthases (AF514287, REGION: 47.1867; Citrus limon) and (AY055214, REGION: 48.1889; Agastache rugosa) and (-)-limonene synthases (DQ195275, REGION: 1.1905; Picea sitchensis), (AF006193, REGION: 73.1986;Abies grandis), and (MHC4SLSP, REGION: 29.1828; Mentha spicata). In some embodiments, the heterologous nucleotide encodes a myrcene synthase. Illustrative examples of suitable nucleotide sequences include, but are not limited to: (U87908; Abies grandis), (A Yl 95609; Antirrhinum majus), (A Yl 95608; Antirrhinum majus), (NM_l27982; Arabidopsis thaliana TPSlO), (NM_ll3485; Arabidopsis thaliana ATTPS-CIN), (NM_ 113483; Arabidopsis thaliana ATTPS-CIN), (AF271259; Perilla frutescens), (AY473626; Picea abies), (AF369919; Picea abies), and (AJ304839; Quercus ilex). In some embodiments, the heterologous nucleotide encodes an ocimene synthase. Illustrative examples of suitable nucleotide sequences include, but are not limited to: (AYl 95607; Antirrhinum majus), (A Yl 95609; Antirrhinum majus), (A Yl 95608; Antirrhinum majus), (AK221024; Arabidopsis thaliana), (NM_ 113485; Arabidopsis thaliana ATTPS-CIN), (NM_ll3483; Arabidopsis thaliana ATTPS- ATTORNEY DOCKET: 51494-029WO2 PATENT CIN), (NM_ll 7775; Arabidopsis thaliana ATTPS03), (NM_001036574; Arabidopsis thaliana ATTPS03), (NM_l27982; Arabidopsis thaliana TPS 10), (AB 110642; Citrus unshiu CitMTSL4), and (AY575970; Lotus corniculatus var. Japonicus ). In some embodiments, the heterologous nucleotide encodes an aα-pinene synthase. Illustrative examples of suitable nucleotide sequences include but are not limited to: (+) α-pinene synthase (AF543530, REGION: 1.1887; Pinus taeda), (-) α-pinene synthase (AF543527, REGION: 32.1921; Pinus taeda), and (+)/ (-)a-pinene synthase (AGU87909, REGION: 6111892;Abies grandis). In some embodiments, the heterologous nucleotide encodes a P-pinene synthase. Illustrative examples of suitable nucleotide sequences include but are not limited to: (-) Ppinene synthases (AF276072, REGION: 1.1749; Artemisia annua) and (AF514288, REGION: 26.1834; Citrus limon). In some embodiments, the heterologous nucleotide encodes a sabinene synthase. An illustrative example of a suitable nucleotide sequence includes but is not limited to AF05 l 901, REGION: 26.1798 from Salvia ofjicinalis. In some embodiments, the heterologous nucleotide encodes a y-terpinene synthase. Illustrative examples of suitable nucleotide sequences include, but are not limited to: (AF514286, REGION: 30.1832 from Citrus limon) and (ABl 10640, REGION 1.1803 from Citrus unshiu). In some embodiments, the heterologous nucleotide encodes a terpinolene synthase. Illustrative examples of a suitable nucleotide sequence include but are not limited to: (AY693650 from Ocimum basilicum) and (AY906866, REGION: 10.1887 from Pseudotsuga menziesii). In some embodiments, the heterologous nucleotide encodes an amorphadiene synthase. An illustrative example of a suitable nucleotide sequence is SEQ ID NO.37 of U.S. Patent Publication No. 2004/0005678. In some embodiments, the heterologous nucleotide encodes an α-farnesene synthase. Illustrative examples of suitable nucleotide sequences include but are not limited to DQ309034 from Pyrus communis cultivar d'Anjou (pear; gene name AFSl) and AY182241 from Malus domestica (apple; gene AFSl). Pechouus et al., Planta 219(1):84-94 (2004). In some embodiments, the heterologous nucleotide encodes a β-farnesene synthase. Illustrative examples of suitable nucleotide sequences include but are not limited to GenBank accession number AF024615 from Mentha x piperita (peppermint; gene Tspal 1), and A Y835398 from Artemisia annua. Picaud et al., Phytochemistry 66(9): 961-967 (2005). In some embodiments, the heterologous nucleotide encodes a farnesol synthase. Illustrative examples of suitable nucleotide sequences include but are not limited to GenBank accession number AF529266 from Zea mays and YDR481C from Saccharomyces cerevisiae (gene Pho8). Song, L., Applied Biochemistry and Biotechnology 128: 149-158 (2006). In some embodiments, the heterologous nucleotide encodes a nerolidol synthase. An illustrative example of a suitable nucleotide sequence includes but is not limited to AF529266 from Zea mays (maize; gene tpsl). In some embodiments, the heterologous nucleotide encodes a patchoulol synthase. Illustrative examples of suitable nucleotide sequences include but are not limited to AY508730 REGION: 1.1659 from Pogostemon cablin. ATTORNEY DOCKET: 51494-029WO2 PATENT In some embodiments, the heterologous nucleotide encodes a nootkatone synthase. Illustrative examples of a suitable nucleotide sequence include but are not limited to AF441124 REGION: 1.1647 from Citrus sinensis and AY917195 REGION: 1.1653 from Perilla frutescens. In some embodiments, the heterologous nucleotide encodes an abietadiene synthase. Illustrative examples of suitable nucleotide sequences In some embodiments, one or more heterologous nucleic acids encoding one or more enzymes are integrated into the genome of the cell. In some embodiments, one or more heterologous nucleic acids encoding one or more enzymes are present within one or more plasmids. Cannabinoid Biosynthetic Pathway The cell may include one or more nucleic acids encoding one or more enzymes of a heterologous genetic pathway that produces a cannabinoid or a precursor of a cannabinoid. The cannabinoid biosynthetic pathway may begin with hexanoic acid as the substrate for an acyl activating enzyme (AAE) to produce hexanoyl-CoA, which is used as the substrate of a tetraketide synthase (TKS) to produce tetraketide-CoA, which is used by an olivetolic acid cyclase (OAC) to produce olivetolic acid, which is then used to produce a cannabigerolic acid by a geranyl pyrophosphate (GPP) synthase and a cannabigerolic acid synthase (CBGaS). In some embodiments, the cannabinoid precursor that is produced is a substrate in the cannabinoid pathway (e.g., hexanoate or olivetolic acid). In some embodiments, the precursor is a substrate for an AAE, a TKS, an OAC, a CBGaS, or a GPP synthase. In some embodiments, the precursor, substrate, or intermediate in the cannabinoid pathway is hexanoate, olivetol, or olivetolic acid. In some embodiments, the precursor is hexanoate. In some embodiments, the cell does not contain the precursor, substrate or intermediate in an amount sufficient to produce the cannabinoid or a precursor of the cannabinoid. In some embodiments, the cell does not contain hexanoate at a level or in an amount sufficient to produce the cannabinoid in an amount over 10 mg/L. In some embodiments, the heterologous genetic pathway encodes at least one enzyme selected from the group consisting of an AAE, a TKS, an OAC, a CBGaS, or a GPP synthase. In some embodiments, the genetically modified cell includes an AAE, TKS, OAC, CBGaS, and a GPP synthase. The cannabinoid pathway is described in Keasling et al., U.S. Patent No.10,563,211, the disclosure of which is incorporated herein by reference. The cell may include, in some embodiments, a heterologous AAE such that the cell is capable of producing a cannabinoid. The AAE may be from Cannabis sativa or may be an enzyme from another plant or fungal source which has been shown to have AAE activity in the cannabinoid biosynthetic pathway, resulting in the production of the cannabinoid precursor olivetolic acid In some embodiments, the cell may include a heterologous TKS such that the cell is capable of producing a cannabinoid. A TKS uses the hexanoyl-CoA precursor to generate tetraketide-CoA. The TKS may be from Cannabis sativa or may be an enzyme from another plant or fungal source which has been shown to have TKS activity in the cannabinoid biosynthetic pathway, resulting in the production of the cannabinoid precursor olivetolic acid. Some embodiments concern a cell that includes a heterologous CBGaS such that the cell is capable of producing a cannabinoid. A CBGaS uses the olivetolic acid precursor and GPP precursor to generate cannabigerolic acid. The CBGaS may be from Cannabis sativa or may be an enzyme from ATTORNEY DOCKET: 51494-029WO2 PATENT another plant or fungal source which has been shown to have CBGaS activity in the cannabinoid biosynthetic pathway, resulting in the production of the cannabinoid cannabigerolic acid. Some embodiments concern a cell that includes a heterologous GPP synthase such that the cell is capable of producing a cannabinoid. A GPP synthase uses the product of the isoprenoid biosynthesis pathway precursor to generate cannabigerolic acid together with a prenyltransferase enzyme. The GPP synthase may be from Cannabis sativa or may be an enzyme from another plant or bacterial source which has been shown to have GPP synthase activity in the cannabinoid biosynthetic pathway, resulting in the production of the cannabinoid cannabigerolic acid. The population of cells may further express other heterologous enzymes in addition to the AAE, TKS, CBGaS, and/or GPP synthase. For example, in some embodiments, the cell may include a heterologous nucleic acid that encodes at least one enzyme from the mevalonate biosynthetic pathway. Enzymes which make up the mevalonate biosynthetic pathway may include but are not limited to an acetyl-CoA thiolase, an HMG-CoA synthase, an HMG-CoA reductase, a mevalonate kinase, a phosphomevalonate kinase, a mevalonate pyrophosphate decarboxylase, and an IPP: DMAPP isomerase. In some embodiments, the cell includes a heterologous nucleic acid that encodes the acetyl- CoA thiolase, the HMG-CoA synthase, the HMG-CoA reductase, the mevalonate kinase, the phosphomevalonate kinase, the mevalonate pyrophosphate decarboxylase, and the IPP: DMAPP isomerase of the mevalonate biosynthesis pathway. In some embodiments, the cell may include an olivetolic acid cyclase (OAC) as part of the cannabinoid biosynthetic pathway. In some embodiments, the cell further includes one or more heterologous nucleic acids that each, independently, encode an acetyl-CoA synthase, and/or an aldehyde dehydrogenase, and/or a pyruvate decarboxylase. In some embodiments, the cell contains a heterologous nucleic acid encoding an aceto-CoA carboxylase (ACC). In some embodiments, the cell contains a heterologous nucleic acid encoding an ACC and an acetoacetyl-CoA synthase (AACS) instead of a heterologous nucleic acid encoding an acetyl-CoA thiolase. Human Milk Oligosaccharide Biosynthetic Pathway In addition to being modified so as to be deficient in expression and/or activity of one or more endogenous oxidoreductases (e.g., one or more endogenous aldose reductases described herein), cells of the disclosure may also be modified so as to express the enzymes of the biosynthetic pathway of a target HMO. In some embodiments, for example, cells of the disclosure (e.g., yeast cells) may naturally express some of the enzymes of the biosynthetic pathway for a given HMO. Such cells may be modified to express the remaining enzymes of the biosynthetic pathway. In some embodiments, for instance, a cell (e.g., a yeast cell) may naturally express many of the enzymes of the biosynthetic pathway of a desired HMO, and the cells may be modified so as to express the remaining enzymes of the biosynthetic pathway for the desired HMO by providing the cells with one or more heterologous nucleic acid molecules that, together, encode the remaining enzymes of the biosynthetic pathway. ATTORNEY DOCKET: 51494-029WO2 PATENT In some embodiments, cells of the disclosure are provided with heterologous nucleic acid molecules that encode one or more enzymes of a pathway for synthesizing LNnT, including a β-1,3-N- acetylglucosaminyltransferase (LgtA), a β-1,4-galactosyltransferase (LgtB), and a UDP-N- acetylglucosamine diphosphorylase. Exemplary LgtA and LgtB enzymes useful in conjunction with the compositions and methods of the disclosure are described in the sections that follow. In some embodiments, cells of the disclosure are provided with heterologous nucleic acid molecules that encode one or more enzymes of a pathway for synthesizing 2’-FL, including a lactose permease, a GDP-mannose 4,6-dehydratase, a GDP-L-fucose synthase, an α-1,2-fucosyltransferase, and a fucosidase. Exemplary enzymes useful in conjunction with the compositions and methods of the disclosure are described in the sections that follow. In some embodiments, cells of the disclosure are provided with heterologous nucleic acid molecules that encode one or more enzymes of a pathway for synthesizing 3-fucosyllactose, including a GDP-mannose 4,6-dehydratase, a GDP-L-fucose synthase, an α-1,3-fucosyltransferase, and a fucosidase. Exemplary enzymes useful in conjunction with the compositions and methods of the disclosure are described in the sections that follow. In some embodiments, cells of the disclosure are provided with heterologous nucleic acid molecules that encode one or more enzymes of a pathway for synthesizing lacto-N-tetraose, including a β-1,3-N-acetylglucosaminyltransferase, a β-1,3-galactosyltransferase, and a UDP-N-acetylglucosamine diphosphorylase. Exemplary enzymes useful in conjunction with the compositions and methods of the disclosure are described in the sections that follow. In some embodiments, cells of the disclosure are provided with heterologous nucleic acid molecules that encode one or more enzymes of a pathway for synthesizing 3’-sialyllactose, including a CMP-Neu5Ac synthetase, a sialic acid synthase, a UDP-N-acetylglucosamine 2-epimerase, a UDP-N- acetylglucosamine diphosphorylase, and a CMP-N-acetylneuraminate-β-galactosamide-α-2,3- sialyltransferase. Exemplary enzymes useful in conjunction with the compositions and methods of the disclosure are described in the sections that follow. In some embodiments, cells of the disclosure are provided with heterologous nucleic acid molecules that encode one or more enzymes of a pathway for synthesizing 6’-sialyllactose, including a CMP-Neu5Ac synthetase, a sialic acid synthase, a UDP-N-acetylglucosamine 2-epimerase, a UDP-N- acetylglucosamine diphosphorylase, and a β-galactoside-α-2,6-sialyltransferase. Exemplary enzymes useful in conjunction with the compositions and methods of the disclosure are described in the sections that follow. In some embodiments, cells of the disclosure are provided with heterologous nucleic acid molecules that encode one or more enzymes of a pathway for synthesizing difucosyllactose, including a GDP-mannose 4,6-dehydratase, a GDP-L-fucose synthase, an α-1,2-fucosyltransferase, and an α-1,3- fucosyltransferase. Exemplary enzymes useful in conjunction with the compositions and methods of the disclosure are described in the sections that follow. In some embodiments, the cells of the disclosure express an LgtA polypeptide. The LgtA polypeptides of the disclosure can be used to produce one or more of a variety of HMOs, including, without limitation, LNnT, LNT, LNFP I, LNFP II, LNFP III, LNFP V, LNFP VI, LNDFH I, LNDFH II, LNH, ATTORNEY DOCKET: 51494-029WO2 PATENT LNnH, F-LNH I, F-LNH II, DFLNH I, DFLNH II, DFLNnH, DF-para-LNH, DF-para-LNnH, TF-LNH, LST a, LST b, LST c, DS-LNT, F-LST a, F-LST b, FS-LNH, FS-LNnH I, and FDS-LNH II. In some embodiments, the cells of the disclosure express a LgtB polypeptide. In some embodiments, the cells of the disclosure express a protein that transports lactose into the cell. In some embodiments, the cells of the disclosure express a GDP-mannose 4,6-dehydratase. In some embodiments, the cells of the disclosure express a GDP-L-fucose synthase. In some embodiments, the cells of the disclosure express an α-1,2-fucosyltransferase polypeptide. Steviol Glycoside Biosynthetic Pathway In some embodiments, the cells are capable of producing one or more steviol glycosides may encode on or more enzymes of the steviol glycoside biosynthesis pathway. In some embodiments, the steviol glycoside biosynthesis pathway is activated in the genetically modified cells by engineering the cells to express polynucleotides encoding enzymes capable of catalyzing the biosynthesis of steviol glycosides. In some embodiments, the genetically modified cells contain one or more heterologous polynucleotides encoding a geranylgeranyl diphosphate synthase (GGPPS), a copalyl diphosphate synthase (CDPS), a kaurene synthase (KS), a kaurene oxidase (KO), a kaurene acid hydroxylase (KAH), a cytochrome P450 reductase (CPR), and/or one or more additional UDP-glycosyltransferases, such as UGT74G1, UGT76G1, UGT85C2, UGT91D, EUGT11, and/or UGT40087. In some embodiments, the genetically modified cells contain one or more heterologous polynucleotides encoding a variant GGPPS, CDPS, KS, KO, KAH, CPR, UDP-glycosyltransferase, UGT74G1, UGT76G1, UGT85C2, UGT91D, EUGT11, and/or UGT40087. In certain embodiments, the variant enzyme may have from 1 up to 20 (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 1313, 15, 16, 17, 18, 19, or 20) amino acid substitutions relative to a reference enzyme. In certain embodiments, the coding sequence of the polynucleotide is codon optimized for the particular cell. GGPPS (EC 2.5.1.29) catalyzes the conversion of farnesyl pyrophosphate into geranylgeranyl diphosphate. Examples of GGPPS include those of Stevia rebaudiana (accession no. ABD92926), Gibberella fujikuroi (accession no. CAA75568), Mus musculus (accession no. AAH69913), Thalassiosira pseudonana (accession no. XP_002288339), Streptomyces clavuligerus (accession no. ZP-05004570), Sulfulobus acidocaldarius (accession no. BAA43200), Synechococcus sp. (accession no. ABC98596), Arabidopsis thaliana (accession no. MP_195399), and Blakeslea trispora (accession no. AFC92798.1), and those described in U.S. Patent No.9,631,215. CDPS (EC 5.5.1.13) catalyzes the conversion of geranylgeranyl diphosphate into copalyl diphosphate. Examples of copalyl diphosphate synthases include those from Stevia rebaudiana (accession no. AAB87091), Streptomyces clavuligerus (accession no. EDY51667), Bradyrhizobioum japonicum (accession no. AAC28895.1), Zea mays (accession no. AY562490), Arabidopsis thaliana (accession no. NM_116512), and Oryza sativa (accession no. Q5MQ85.1), and those described in U.S. Patent No.9,631,215. In some embodiments, the cell includes a heterologous nucleic acid encoding a CDPS. KS (EC 4.2.3.19) catalyzes the conversion of copalyl diphosphate into kaurene and diphosphate. Examples of enzymes include those of Bradyrhizobium japonicum (accession no. AAC28895.1), ATTORNEY DOCKET: 51494-029WO2 PATENT Arabidopsis thaliana (accession no. Q9SAK2), and Picea glauca (accession no. ADB55711.1), and those described in U.S. Patent No.9,631,215. In some embodiments, the cell includes a heterologous nucleic acid encoding a KS. CDPS-KS bifunctional enzymes (EC 5.5.1.13 and EC 4.2.3.19) may also be used in the cells of the invention. Examples include those of Phomopsis amygdali (accession no. BAG30962), Phaeosphaeria sp. (accession no. O13284), Physcomitrella patens (accession no. BAF61135), and Gibberella fujikuroi (accession no. Q9UVY5.1), and those described in U.S. Patent Application Publication Nos.2014/032928 A1, 2014/0357588 A1, 2015/0159188, and WO 2016/038095. KO (EC 1.14.13.88) catalyzes the conversion of kaurene into kaurenoic acid. Illustrative examples of enzymes include those of Oryza sativa (accession no. Q5Z5R4), Gibberella fujikuroi (accession no. O94142), Arabidopsis thaliana (accession no. Q93ZB2), Stevia rebaudiana (accession no. AAQ63464.1), and Pisum sativum (Uniprot no. Q6XAF4), and those described in U.S. Patent Application Publication Nos.2014/0329281 A1, 2014/0357588 A1, 2015/0159188, and WO 2016/038095. In some embodiments, the cell includes a heterologous nucleic acid encoding a KO. KAH (EC 1.14.13) also referred to as steviol synthases catalyze the conversion of kaurenoic acid into steviol. Examples of enzymes include those of Stevia rebaudiana (accession no. ACD93722), Arabidopsis thaliana (accession no. NP_197872), Vitis vinifera (accession no. XP_002282091), and Medicago trunculata (accession no. ABC59076), and those described in U.S. Patent Application Publication Nos.2014/0329281, 2014/0357588, 2015/0159188, and WO 2016/038095. In some embodiments, the cell includes a heterologous nucleic acid encoding a KAH. A CPR (EC 1.6.2.4) is necessary for the activity of KO and/or KAH above. Examples of enzymes include those of Stevia rebaudiana (accession no. ABB88839), Arabidopsis thaliana (accession no. NP_194183), Gibberella fujikuroi (accession no. CAE09055), and Artemisia annua (accession no. ABC47946.1), and those described in U.S. Patent Application Publication Nos.2014/0329281, 2014/0357588, 2015/0159188, and WO 2016/038095. In some embodiments, the cell includes a heterologous nucleic acid encoding a CPR. UGT74G1 is capable of functioning as a uridine 5’-diphospho glucosyl: steviol 19-COOH transferase and as a uridine 5’-diphospho glucosyl: steviol-13-O-glucoside 19-COOH transferase. Accordingly, UGT74G1 is capable of converting steviol to 19-glycoside; converting steviol to 19-glycoside, steviolmonoside to rubusoside; and steviolbioside to stevioside. UGT74G1 has been described in Richman et al., 2005, Plant J., vol.41, pp.56-67; U.S. Patent Application Publication No.2014/0329281; WO 2016/038095; and accession no. AAR06920.1. In some embodiments, the cell includes a heterologous nucleic acid encoding a UGT74G1. UGT76G1 is capable of transferring a glucose moiety to the C-3’ position of an acceptor molecule a steviol glycoside (where glycoside = Glcb(1 ^2)Glc). This chemistry can occur at either the C-13-O- linked glucose of the acceptor molecule, or the C-19-O-linked glucose acceptor molecule. Accordingly, UGT76G1 is capable of functioning as a uridine 5’-diphospho glucosyltransferase to the: (1) C-3’ position of the 13-O-linked glucose on steviolbioside in a beta linkage forming RebB, (2) C-3’ position of the 19-O- linked glucose on stevioside in a beta linkage forming RebA, and (3) C-3’ position of the 19-O-linked glucose on RebD in a beta linkage forming RebM. UGT76G1 has been described in Richman et al., 2005, Plant J., vol.41, pp.56-67; US2014/0329281; WO2016/038095; and accession no. AAR06912.1. ATTORNEY DOCKET: 51494-029WO2 PATENT UGT85C2 is capable of functioning as a uridine 5’-diphospho glucosyl: steviol 13-OH transferase, and a uridine 5’-diphospho glucosyl: steviol-19-O-glucoside 13-OH transferase. UGT85C2 is capable of converting steviol to steviolmonoside and is also capable of converting 19-glycoside to rubusoside. Examples of UGT85C2 enzymes include those of Stevia rebaudiana: see e.g., Richman et al., (2005), Plant J., vol.41, pp.56-67; U.S. Patent Application Publication No.2014/0329281; WO 2016/038095; and accession no. AAR06916.1. In some embodiments, the cell includes a heterologous nucleic acid encoding a UGT85C2. UGT40087 is capable of transferring a glucose moiety to the C-2’ position of the 19-O-glucose of RebA to produce RebD. UGT40087 is also capable of transferring a glucose moiety to the C-2’ position of the 19-O-glucose of stevioside to produce RebE. Examples of UGT40087 include those of accession no. XP_004982059.1 and WO 2018/031955. In some embodiments, the cell includes a heterologous nucleic acid encoding a UGT40087. Introduction of Heterologous Nucleic Acids into a Host Cell In some embodiments, a heterologous nucleic acid of the disclosure is introduced into a host cell (e.g., yeast cell) by way of a gap repair molecular biology technique. The host cell may be host cell capable of producing a fermentation product or a previously fermented cell. In these methods, if the host cell has non-homologous end joining (NHEJ) activity, as is the case for Kluyveromyces marxianus, then the NHEJ activity in the host cell can be first disrupted in any of a number of ways. Further details related to genetic modification of host cells (e.g., yeast cells) through gap repair can be found in U.S. Patent No. 9,476,065, the disclosure of which is incorporated herein by reference in its entirety. In some embodiments, a heterologous nucleic acid of the disclosure is introduced into the host cell by way of one or more site-specific nucleases capable of causing breaks at designated regions within selected nucleic acid target sites. Examples of such nucleases include, but are not limited to, endonucleases, site-specific recombinases, transposases, topoisomerases, zinc finger nucleases, TAL- effector DNA binding domain-nuclease fusion proteins (TALENs), CRISPR/Cas-associated RNA-guided endonucleases, and meganucleases. Further details related to genetic modification of host cells through site specific nuclease activity can be found in U.S. Patent No.9,476,065, the disclosure of which is incorporated herein by reference in its entirety. Nucleic Acid and Amino Acid Sequence Optimization Described herein are specific genes and proteins useful in the methods, compositions, and organisms of the disclosure; however, it will be recognized that absolute identity to such genes is not necessary. For example, changes in a particular gene or polynucleotide including a sequence encoding a polypeptide or enzyme can be performed and screened for activity. Typically, such changes include conservative mutations and silent mutations. Such modified or mutated polynucleotides and polypeptides can be screened for expression of a functional enzyme using methods known in the art. Due to the inherent degeneracy of the genetic code, other polynucleotides which encode substantially the same or functionally equivalent polypeptides can also be used to clone and express the polynucleotides encoding such enzymes. ATTORNEY DOCKET: 51494-029WO2 PATENT As will be understood by those of skill in the art, it can be advantageous to modify a coding sequence to enhance its expression in a particular host. The genetic code is redundant with 64 possible codons, but most organisms typically use a subset of these codons. The codons that are utilized most often in a species are called optimal codons, and those not utilized very often are classified as rare or low-usage codons. Codons can be substituted to reflect the preferred codon usage of the host, in a process sometimes called "codon optimization" or "controlling for species codon bias." Optimized coding sequences containing codons preferred by a particular prokaryotic or eukaryotic host (Murray et al., 1989, Nucl Acids Res.17: 477-508) can be prepared, for example, to increase the rate of translation or to produce recombinant RNA transcripts having desirable properties, such as a longer half-life, as compared with transcripts produced from a non-optimized sequence. Translation stop codons can also be modified to reflect host preference. For example, typical stop codons for S. cerevisiae and mammals are UAA and UGA, respectively. The typical stop codon for monocotyledonous plants is UGA, whereas insects and E. coli commonly use UAA as the stop codon (Dalphin et al., 1996, Nucl Acids Res.24: 216-8). Those of skill in the art will recognize that, due to the degenerate nature of the genetic code, a variety of DNA molecules differing in their nucleotide sequences can be used to encode a given heterologous polypeptide of the disclosure. A native DNA sequence encoding the biosynthetic enzymes described above is referenced herein merely to illustrate an embodiment of the disclosure, and the disclosure includes DNA molecules of any sequence that encode the amino acid sequences of the polypeptides and proteins of the enzymes utilized in the methods of the disclosure. In similar fashion, a polypeptide can typically tolerate one or more amino acid substitutions, deletions, and insertions in its amino acid sequence without loss or significant loss of a desired activity. The disclosure includes such polypeptides with different amino acid sequences than the specific proteins described herein so long as the modified or variant polypeptides have the enzymatic anabolic or catabolic activity of the reference polypeptide. Furthermore, the amino acid sequences encoded by the DNA sequences shown herein merely illustrate embodiments of the disclosure. When "homologous" is used in reference to proteins or peptides, it is recognized that residue positions that are not identical often differ by conservative amino acid substitutions. A "conservative amino acid substitution" is one in which an amino acid residue is substituted by another amino acid residue having a side chain (R group) with similar chemical properties, e.g., charge or hydrophobicity. In general, a conservative amino acid substitution will not substantially change the functional properties of a protein. In cases where two or more amino acid sequences differ from each other by conservative substitutions, the percent sequence identity or degree of homology may be adjusted upwards to correct for the conservative nature of the substitution. Means for making this adjustment are well known to those of skill in the art (See, e.g., Pearson W. R., 1994, Methods in Mol. Biol.25: 365-89). Furthermore, any of the genes encoding an enzyme described herein (or any of the regulatory elements that control or modulate expression thereof) can be optimized by genetic/protein engineering techniques, such as directed evolution or rational mutagenesis, which are known to those of ordinary skill in the art. Such action allows those of ordinary skill in the art to optimize the enzymes for expression and activity in yeast. ATTORNEY DOCKET: 51494-029WO2 PATENT In addition, genes encoding these enzymes can be identified from other fungal and bacterial species and can be expressed for the modulation of this pathway. A variety of organisms could serve as sources for these enzymes, including, but not limited to, Saccharomyces spp., including S. cerevisiae and S. uvarum, Kluyveromyces spp., including K. thermotolerans, K. lactis, and K. marxianus, Pichia spp., Hansenula spp., including H. polymorpha, Candida spp., Trichosporon spp., Yamadazyma spp., including Y. spp. stipitis, Torulaspora pretoriensis, Issatchenkia orientalis, Schizosaccharomyces spp., including S. pombe, Cryptococcus spp., Aspergillus spp., Neurospora spp., or Ustilago spp. Sources of genes from anaerobic fungi include, but are not limited to, Piromyces spp., Orpinomyces spp., or Neocallimastix spp. Sources of prokaryotic enzymes that are useful include, but are not limited to, Escherichia. coli, Zymomonas mobilis, Staphylococcus aureus, Bacillus spp., Clostridium spp., Corynebacterium spp., Pseudomonas spp., Lactococcus spp., Enterobacter spp., Salmonella spp., or X. dendrorhous. Techniques known to those skilled in the art may be suitable to identify additional homologous genes and homologous enzymes. Generally, analogous genes and/or analogous enzymes can be identified by functional analysis and will have functional similarities. Techniques known to those skilled in the art can be suitable to identify analogous genes and analogous enzymes. Techniques include, but are not limited to, cloning a gene by PCR using primers based on a published sequence of a gene/enzyme of interest, or by degenerate PCR using degenerate primers designed to amplify a conserved region among a gene of interest. Further, one skilled in the art can use techniques to identify homologous or analogous genes, proteins, or enzymes with functional homology or similarity. Techniques include examining a cell or cell culture for the catalytic activity of an enzyme through in vitro enzyme assays for said activity, e.g., as described herein or in Kiritani, K., Branched-Chain Amino Acids Methods Enzymology, 1970; then isolating the enzyme with said activity through purification; determining the protein sequence of the enzyme through techniques such as Edman degradation; design of PCR primers to the likely nucleic acid sequence; amplification of said DNA sequence through PCR; and cloning of said nucleic acid sequence. To identify homologous or similar genes and/or homologous or similar enzymes, suitable techniques also include comparison of data concerning a candidate gene or enzyme with databases such as BRENDA, KEGG, or MetaCYC. The candidate gene or enzyme can be identified within the above-mentioned databases in accordance with the teachings herein. Culture and Fermentation Methods Materials and methods for the maintenance and growth of microbial cultures are well known to those skilled in the art of microbiology or fermentation science (see, for example, Bailey et al., Biochemical Engineering Fundamentals, second edition, McGraw Hill, New York, 1986). Consideration must be given to appropriate culture medium, pH, temperature, and requirements for aerobic, microaerobic, or anaerobic conditions, depending on the specific requirements of the host cell, the fermentation, and the process. The methods of producing squalene provided herein may be performed in a suitable culture medium in a suitable container, including but not limited to a cell culture plate, a flask, or a fermentor. Further, the methods can be performed at any scale of fermentation known in the art to support industrial production of microbial products. Any suitable fermentor may be used including a stirred tank fermentor, an airlift fermentor, a bubble fermentor, or any combination thereof. In particular embodiments utilizing ATTORNEY DOCKET: 51494-029WO2 PATENT Saccharomyces cerevisiae as the host cell, strains can be grown in a fermentor as described in detail by Kosaric, et al, in Ullmann's Encyclopedia of Industrial Chemistry, Sixth Edition, Volume 12, pages 398- 473, Wiley-VCH Verlag GmbH & Co. KDaA, Weinheim, Germany. In some embodiments, the culture medium is any culture medium in which a microorganism capable of producing a heterologous product can subsist, i.e., maintain growth and viability. In some embodiments, the culture medium is an aqueous medium comprising assimilable carbon, nitrogen and phosphate sources. Such a medium can also include appropriate salts, minerals, metals, and other nutrients. In some embodiments, the carbon source and each of the essential cell nutrients are added incrementally or continuously to the fermentation medium, and each required nutrient is maintained at essentially the minimum level needed for efficient assimilation by growing cells, for example, in accordance with a predetermined cell growth curve based on the metabolic or respiratory function of the cells which convert the carbon source to a biomass. Suitable conditions and suitable medium for culturing microorganisms are well known in the art. In some embodiments, the suitable medium is supplemented with one or more additional agents, such as, for example, an inducer (e.g., when one or more nucleotide sequences encoding a gene product are under the control of an inducible promoter), a repressor (e.g., when one or more nucleotide sequences encoding a gene product are under the control of a repressible promoter), or a selection agent (e.g., an antibiotic to select for microorganisms comprising the genetic modifications). Host Cell Strains Any suitable cell may be used in the practice of the present invention as the host cell or previously fermented cell. Illustrative examples of suitable cells include any archae, prokaryotic, or eukaryotic cell. Examples of an archae cell include but are not limited to those belonging to the genera: Aeropyrum, Archaeglobus, Halobacterium, Methanococcus, Methanobacterium, Pyrococcus, Sulfolobus, and Thermoplasma. Illustrative examples of archae strains include but are not limited to: Aeropyrum pernix, Archaeoglobus fulgidus, Methanococcus jannaschii, Methanobacterium thermoautotrophicum, Pyrococcus abyssi, Pyrococcus horikoshii, Thermoplasma acidophilum, Thermoplasma volcanium. Examples of a prokaryotic cell include, but are not limited to those belonging to the genera: Agrobacterium, Alicyclobacillus, Anabaena, Anacystis, Arthrobacter, Azobacter, Bacillus, Brevibacterium, Chromatium, Clostridium, Corynebacterium, Enterobacter, Erwinia, Escherichia, Lactobacillus, Lactococcus, Mesorhizobium, Methylobacterium, Microbacterium, Phormidium, Pseudomonas, Rhodobacter, Rhodopseudomonas, Rhodospirillum, Rhodococcus, Salmonella, Scenedesmun, Serratia, Shigella, Staphlococcus, Strepromyces, Synnecoccus, and Zymomonas. Illustrative examples of prokaryotic bacterial strains include but are not limited to: Bacillus subtilis, Bacillus amyloliquefacines, Brevibacterium ammoniagenes, Brevibacterium immariophilum, Clostridium beigerinckii, Enterobacter sakazakii, Escherichia coli, Lactococcus lactis, Mesorhizobium loti, Pseudomonas aeruginosa, Pseudomonas mevalonii, Pseudomonas pudica, Rhodobacter capsulatus, Rhodobacter sphaeroides, Rhodospirillum rubrum, Salmonella enterica, Salmonella typhi, Salmonella typhimurium, Shigella dysenteriae, Shigella flexneri, Shigella sonnei, Staphylococcus aureus, and the like. ATTORNEY DOCKET: 51494-029WO2 PATENT In general, if a bacterial host cell is used, a non-pathogenic strain is preferred. Illustrative examples of non-pathogenic strains include but are not limited to: Bacillus subtilis, Escherichia coli, Lactibacillus acidophilus, Lactobacillus helveticus, Pseudomonas aeruginosa, Pseudomonas mevalonii, Pseudomonas pudita, Rhodobacter sphaeroides, Rodobacter capsulatus, Rhodospirillum rubrum, and the like. Examples of eukaryotic cells include but are not limited to fungal cells. Examples of fungal cell include but are not limited to those belonging to the genera: Aspergillus, Candida, Chrysosporium, Cryotococcus, Fusarium, Kluyveromyces, Neotyphodium, Neurospora, Penicillium, Pichia, Saccharomyces, Trichoderma and Xanthophyllomyces (formerly Phaffia). Illustrative examples of eukaryotic strains include but are not limited to: Aspergillus nidulans, Aspergillus niger, Aspergillus oryzae, Candida albicans, Chrysosporium lucknowense, Fusarium graminearum, Fusarium venenatum, Kluyveromyces lactis, Neurospora crassa, Pichia angusta, Pichia finlandica, Pichia kodamae, Pichia membranaefaciens, Pichia methanolica, Pichia opuntiae, Pichia pastoris, Pichia pijperi, Pichia quercuum, Pichia salictaria, Pichia thermotolerans, Pichia trehalophila, Pichia stipitis, Streptomyces ambofaciens, Streptomyces aureofaciens, Streptomyces aureus, Saccaromyces bayanus, Saccaromyces boulardi, Saccharomyces cerevisiae, Streptomyces fungicidicus, Streptomyces griseochromogenes, Streptomyces griseus, Streptomyces lividans, Streptomyces olivogriseus, Streptomyces rameus, Streptomyces tanashiensis, Streptomyces vinaceus, Trichoderma reesei and Xanthophyllomyces dendrorhous (formerly Phaffia rhodozyma). In some embodiments of the present disclosure, the host cell is a yeast cell. In some embodiments, the previously fermented cell is a yeast cell. Yeast cells useful in conjunction with the compositions and methods described herein include yeast that have been deposited with microorganism depositories (e.g. IFO, ATCC, etc.), such as those that belong to the genera Aciculoconidium, Ambrosiozyma, Arthroascus, Arxiozyma, Ashbya, Babjevia, Bensingtonia, Botryoascus, Botryozyma, Brettanomyces, Bullera, Bulleromyces, Candida, Citeromyces, Clavispora, Cryptococcus, Cystofilobasidium, Debaryomyces, Dekkara, Dipodascopsis, Dipodascus, Eeniella, Endomycopsella, Eremascus, Eremothecium, Erythrobasidium, Fellomyces, Filobasidium, Galactomyces, Geotrichum, Guilliermondella, Hanseniaspora, Hansenula, Hasegawaea, Holtermannia, Hormoascus, Hyphopichia, Issatchenkia, Kloeckera, Kloeckeraspora, Kluyveromyces, Kondoa, Kuraishia, Kurtzmanomyces, Leucosporidium, Lipomyces, Lodderomyces, Malassezia, Metschnikowia, Mrakia, Myxozyma, Nadsonia, Nakazawaea, Nematospora, Ogataea, Oosporidium, Pachysolen, Phachytichospora, Phaffia, Pichia, Rhodosporidium, Rhodotorula, Saccharomyces, Saccharomycodes, Saccharomycopsis, Saitoella, Sakaguchia, Saturnospora, Schizoblastosporion, chizosaccharomyces, Schwanniomyces, Sporidiobolus, Sporobolomyces, Sporopachydermia, Stephanoascus, Sterigmatomyces, Sterigmatosporidium, Symbiotaphrina, Sympodiomyces, Sympodiomycopsis, Torulaspora, Trichosporiella, Trichosporon, Trigonopsis, Tsuchiyaea, Udeniomyces, Waltomyces, Wickerhamia, Wickerhamiella, Williopsis, Yamadazyma, Yarrowia, Zygoascus, Zygosaccharomyces, Zygowilliopsis, and Zygozyma, among others. In some embodiments, the strain is Saccharomyces cerevisiae, Pichia pastoris, Schizosaccharomyces pombe, Dekkera bruxellensis, Kluyveromyces lactis (previously called Saccharomyces lactis), Kluveromyces marxianus, Arxula adeninivorans, or Hansenula polymorphs (now known as Pichia angusta). In some embodiments, the host-microbe is a strain of the genus Candida, ATTORNEY DOCKET: 51494-029WO2 PATENT such as Candida lipolytica, Candida guilliermondii, Candida krusei, Candida pseudotropicalis, or Candida utilis. In a particular embodiment, the strain is Saccharomyces cerevisiae. In some embodiments, the host is a strain of Saccharomyces cerevisiae selected from the group consisting of Baker's yeast, CEN.PK, CEN.PK2, CBS 7959, CBS 7960, CBS 7961, CBS 7962, CBS 7963, CBS 7964, IZ-1904, TA, BG-1, CR-1, SA-1, M-26, Y-904, PE-2, PE-5, VR-1, BR-1, BR-2, ME-2, VR-2, MA-3, MA-4, CAT-1, CB-1, NR-1, BT-1, and AL-1. In some embodiments, the strain of Saccharomyces cerevisiae is CEN.PK. In some embodiments, the yeast strain used is Y21900. In some embodiments, the yeast strain used is Y23508. In some embodiments, the strain is a microbe that is suitable for industrial fermentation. In particular embodiments, the microbe is conditioned to subsist under high solvent concentration, high temperature, expanded substrate utilization, nutrient limitation, osmotic stress due to sugar and salts, acidity, sulfite and bacterial contamination, or combinations thereof, which are recognized stress conditions of the industrial fermentation environment. Examples The following examples are put forth so as to provide those of ordinary skill in the art with a description of how the compositions and methods described herein may be used, made, and evaluated, and are intended to be purely exemplary of the invention and are not intended to limit the scope of what the inventors regard as their invention. Example 1. Purification of Polyurethane from a β-Farnesene Distillation Residue Overview To enable the use of biomass-containing polyols derived from industrial fermentation, we first developed processes that prepared these co-products for polymerization reactions. The industrial production of β-farnesene results in a considerable amount of residue labelled as Farnesene Distillation Residue (FDR), which may have great biosynthetic potential as a source of β-farnesene-derived monomers to be used in the development of new bio-based materials. In fact, FDR is a residue rich in β- farnesene, farnesol, other terpenes, phytosterols, fatty alcohols and fatty acids, wax esters, and a polymeric fraction, that, due to their polyol nature, can be used in the obtention of bio-based materials, namely polyurethanes (FIG.1). The presence of sludge and waxy materials, as well as other biomolecules, may interfere with the polymerization of the above materials with isocyanates. Accordingly, FDR generally requires purification. This is, by itself, an important tool in the valorization of all fractions of the FDR. In the first step of the purification process, the fraction useful for the development of the new bio-based materials, which was designated here as Non-Distillate 1 (ND1), was obtained. The oil fraction can be also isolated by a winterization process with ethanol at low temperatures. During this process, the waxy material forms a precipitate while the oil fraction remains dissolved in the ethanolic phase and is recovered by centrifugation. The ND1 fraction was rich in β-farnesene derived monomers, namely hydroxylated derivatives that gave the ND1 fraction the status of polyol. This polyol nature was useful for the development of new ATTORNEY DOCKET: 51494-029WO2 PATENT bio-based polyurethanes, by the reaction of ND1 with different isocyanates. These compounds are commonly used on the synthesis of this type of polymers, being the most common 2,4 – toluene diisocyanate (TDI), methylene diphenyl diisocyanate (MDI), hexamethylene diisocyanate (HDI) and isophorone diisocyanate (IPDI) (FIG.2). In this work, new bio-based polyurethanes from ND1 (bio-based polyol source) were developed with the mentioned isocyanates to produce films. The physicochemical, thermal, barrier and mechanical properties were evaluated to characterize the new materials to define the optimal field of application for each material. After the study of the composition of FDR, it was possible to identify compounds that can be valuable in the field of biopolymers development. The following sections describe the developed procedure to prepare the FDR for the distillation step and the purification itself according to boiling points under vacuum (i.e., short-path distillation). To isolate the oil fraction from FDR residue, two different procedures were used. The first approach was performed by a winterization process in which the FDR residue was dissolved in ethanol and then cooled to a very low temperature (i.e., -30 °C). The other approach consisted of a multi-step filtration procedure. This approach was solvent-free since no organic solvents are used during the process. In both procedures the oil fraction of FDR was isolated from the wax fraction resulting in a good yield and did not result in a significant loss of material. Winterization Step The winterization step was performed by taking 200 g of the raw FDR in a glass container and adding ethanol (food grade) in a portion of 1:4 (w:v, 800 mL). The mixture was shaken for 5 minutes and was left to stand at room temperature for 2 hours. The container was then placed at -30 °C overnight. The mixture was then transferred to centrifuge tubes and centrifuged at 1250 g for 10 minutes at room temperature. The resulting oil fraction in the ethanolic phase was collected and kept in the vacuum oven at 60°C and 50 mbar for 24 hours (or until the weight remained constant). Oil and waxes were obtained with yields of 90% and 10% respectively, and no significant losses were registered in this process. Multi-Step Filtration The multi-step filtration was performed by filtering the FDR in three steps to separate the wax fraction from the oil fraction. This was performed by taking 475 g of FDR residue and filtering it through a TNT filter (Tescoma), followed by filtering the filtrate through an 11μm filter, and finally by filtering the filtrate through an 8 μm filter. All the filtration steps were executed under vacuum. In this process, the oil fraction was obtained with a yield of 80% while the wax fraction made up 15%, and around 5% of the material was lost in the process, most likely in the glassware and filters Short Path Distillation Step To increase the purity of the substrate and improve the polymerization reaction, the oil fraction, which contained the polyols required for the polymerization process, was further processed by means of a short path distillation procedure to isolate ND1 from the other fractions of interest. This was performed by taking 258 g of the oil fraction, previously isolated by winterization or filtration, and adding it to the short ATTORNEY DOCKET: 51494-029WO2 PATENT path distillation apparatus. Distillation was achieved using a temperature of 180°C, a pressure of 0.1 mbar, a feed rate of 1.5 mL/min, and a rotor rotation rate of 350 rpm. The ND1 fraction containing the purified polyols was obtained with a 60% of yield. A distillate (D1) was also obtained representing 27% of yield. Synthesis procedure of polyurethane films. The synthesis of the polyurethane films was carried out by mixing filtered ND1 (3 g) with the isocyanate (TDI, MDI, HDI or IPDI) in a proportion of 7:3 (w/w), 2 % (w) of vinyltrimethoxy silane (VTMS) to avoid interferences in the reaction from humidity and improve brightness, and, in when the isocyanates HDI or IPDI were used, 0.2 %(w) of dibutyltin dilaurate (DBTDL) as the catalyst. The reaction was carried out at 70 °C for 3 hours and was then spread on a glass surface and kept in a fume hood for 48 hours at room temperature to dry the excess isocyanate (FIG.2). The reaction was monitored using FTIR analysis, which followed the formation of the band around 1710 cm ^-1 related to the carbonyl group (C=O), which was characteristic of the urethane linkage formation (FIG.3). After drying the excess of the isocyanate, which did not react, the polyurethane film was ready to be characterized and tested. The drying step was also monitored by FTIR analysis following the disappearance of the band related to the isocyanate group (NCO) around 2265 cm ^-1 (FIG.3). Results Structure analysis by FTIR-ATR After synthesizing polyurethane with different isocyanates, films of new bio-based polyurethane materials were obtained (FIG.1). The formation of the urethane bond was evaluated using FTIR-ATR (FIG.2) where the presence of the main bands related to the urethane linkage formation (C=O stretching around 1712 cm ^-1 and N-H around 3340 cm ^-1 ) were observed. As expected, other important bands were observed which were related with the different structures of the isocyanates used. Thermal Properties analysis by DSC DSC analysis was performed to observe the thermal properties for the different polyurethane films produced and the ND1 fraction. The results obtained are presented in Table 1. Table 1. Thermal transitions obtained by Differential Scanning Calorimetry for the ND1 fraction and different bio-based polyurethane films developed. The thermal properties were important to assess as they provided information regarding the range of temperatures for which the film may be used. For example, the application range was between the temperature of processing (Tm) and the temperature above which the material starts its degradation (T _degradation ) (i.e., T _g ˂ application range > T _m ). Table 1 shows the thermal properties of ND1 fraction and ATTORNEY DOCKET: 51494-029WO2 PATENT all the bio-based polyurethanes produced obtained by the analysis by DSC. The ND1 fraction had a cold crystallization temperature of -46.1 ± 0.1 °C, a melting temperature of -9.2 ± 0.1 °C, and degradation temperature of 390.4 ± 0.2 °C. With the production of the new polyurethane biomaterials, characteristic thermal transitions were assessed, namely the glass transition temperature (T _g ), the curing temperature (T _cure ) as well as the melting (T _melting ), and the decomposition temperature (T _{decomposition} ). For all the biomaterials, the temperature of the glass transition was around -10.1 ± 0.1 °C. The curing temperature was also observed for all the biomaterials including polyurethane films reacted with: HDI (149.8 ± 1.9 °C), IPDI (155.5 ± 0.2 °C), MDI (161.0 ± 13.5 °C), and TDI (194.9 ± 2.1 °C). The curing process is related to the formation of reticulations between polymer chains and can occur at room temperature, which requires a long time. Nevertheless, at the temperatures observed for the curing process, the curing process could be accelerated, and the maximum degree of reticulations could be achieved in less time. Regarding the melting temperatures, all the new biomaterials presented high melting temperatures. Biomaterials made with HDI showed melting temperatures at 250.8 ± 0.4 °C and 332.7 ± 1.1 °C. Biomaterials made with TDI had a melting temperature at 299.9 ± 1.6 °C. Biomaterials made with MDI had a melting temperature at 328 ± 3.0 °C, and made with IPDI had a melting temperature at 340.3 ± 3.5 °C. The decomposition (T _degradation ) of the biomaterials was also observed during the analysis and showed that degradation was higher than 387 °C for all biomaterials. It is important to note that the structure of the isocyanate influenced the thermal transitions observed once the ND1 fraction (polyol) used is always the same. XRD analysis X-ray diffraction (XRD) is a characterization technique that can provide direct evidence of crystalline and/or amorphous structure of the materials. To evaluate the new bio-based polyurethane films in terms of amorphous/crystalline structure when compared with other polyurethanes, XRD analysis was performed. The x-ray diffraction patterns are shown in FIG.4. In general, all the bio-based polyurethanes showed a XRD diffraction pattern characteristic of a material having a low degree of crystallinity as shown by the appearance of broad diffraction peaks at 2θ angles. The polyurethane materials derived from TDI and MDI showed broad peaks at 19° and 43°. In the case of the materials derived from the HDI, broad peaks were observed at 7°, 12°, 19° and 43°. The materials derived from IPDI showed broad peaks at 7°, 17.5° and 43°. The differences in the angles observed were related to the structure of the different isocyanates used and consequently the different patterns of X-ray diffraction and degree of crystallinity. These results indicated that the new bio-based polyurethanes have competitive properties when compared with petroleum-based analogues. Mechanical Properties – Young Modulus and Elongation at Break The Young Modulus as well as the Percentage of Elongation at Break of each material was assessed using a Texturometer and by performing tensile tests. The results are presented in Table 2. The Young Modulus is a measure of the ability of a material to withstand changes in length when under lengthwise tension or compression. The percentage of elongation at break is a measurement that showed how much a material can be stretched, as a percentage of its original dimensions, before it broke. ATTORNEY DOCKET: 51494-029WO2 PATENT Table 2. Mechanical properties of bio-based polyurethanes. Sample Young Modulus (MPa) Elongation at Break (%) P _{U_TDI} ^{3.41 ± 0.67 150.12 ± 9.64} P _{U_MDI} ^{0.44 ± 0.03 64.23 ± 14.14} P _{U_HDI} ^{0.61 ± 0.09 89.93 ± 3.25} P _{U_IPDI} ^{0.27 ± 0.07 665.01 ± 50.20} Different mechanical properties were achieved using ND1 and various isocyanates. For example, the polyurethane made using TDI had a Young Modulus of 3.41 ± 0.67 MPa. This value was comparable with a Young Modulus of a plastic material. The Young Modulus values obtained of the polyurethane films made using other isocyanates were more comparable with elastomers. Regarding the percentage of elongation at break, it was observed that polyurethane film made with IPDI was very stretchable and had a high percentage of elongation before break (665.01 ± 50.20 %) when compared with the other polyurethane samples that present lower percentages of elongation. High percentage of elongation associated to low Young’s Modulus indicated that that the material had good elasticity. Other Embodiments All publications, patents, and patent applications mentioned in this specification are incorporated herein by reference to the same extent as if each independent publication or patent application was specifically and individually indicated to be incorporated by reference. While the invention has been described in connection with specific embodiments thereof, it will be understood that it is capable of further modifications and this application is intended to cover any variations, uses, or adaptations of the invention following, in general, the principles of the invention and including such departures from the invention that come within known or customary practice within the art to which the invention pertains and may be applied to the essential features hereinbefore set forth, and follows in the scope of the claims. Other embodiments are within the claims.