Methods for improved cell culture performance and product recovery

Abstract

The present disclosure relates to the production of organic compounds by host cell cultures, in particular, organic compounds which are inhibitory to host cells and / or are susceptible to chemical modification, including degradation and / or oxidation, in cell culture conditions. Improved systems and methods are herein disclosed for alleviating inhibition of host cells caused by product accumulation in the culture medium, thereby enhancing cell health and performance, including, for example, increased yield and productivity. Product recovery and purity are furthermore improved.

Description

[0001]Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT METHODS FOR IMPROVED CELL CULTURE PERFORMANCE AND PRODUCT RECOVERY STATEMENT OF RIGHTS TO INVENTIONS MADE UNDER FEDERALLY SPONSORED RESEARCH This invention was made with government support under Cooperative Agreement Number FA8650-21-2-5028 awarded by the Department of Defense. The government has certain rights in the invention. FIELD OF THE INVENTION The present disclosure relates to methods to produce and recover organic compounds produced during the course of a fermentation process or other method of cell culture. BACKGROUND In the field of synthetic biology, microorganisms are genetically modified to produce a target molecule of interest. Once produced, the molecule of interest may be extracted and purified from the culture medium. In some cases, such as with monoterpenes (e.g., myrcene, limonene, linalool), the molecule of interest may negatively impact host cell metabolism and product production. Thus, as the host cells produce the molecule, product accumulation in the culture medium becomes inhibitory to host cells, ultimately decreasing yield and productivity for the molecule. In addition, products that are susceptible to chemical modification in the culture medium may degrade and / or oxidize over the course of several days in the fermentation environment, further reducing yield and / or purity. Thus, there is a need in the art for improved systems and methods for producing molecules of interest by genetically modified host cells, in particular, when the molecules of interest are inhibitory to the host cells and / or are sensitive to degradation and / or oxidation in cell culture conditions. SUMMARY OF THE INVENTION Provided herein are methods for producing and recovering molecules of interest produced by genetically modified host cells. The methods disclosed herein can be used, for example, in connection with molecules that are inhibitory to the host cells, such as, for example, monoterpenes (e.g., myrcene, limonene, linalool). By removing the inhibitory molecules from the culture medium as they are being produced, inhibition of the host cells is alleviated and as a result, cell health and ultimately yield and productivity can be maintained and / or improved. In addition, by sequestering the product from the culture medium, product degradation and / or oxidation may be prevented or reduced, further improving yield and purity. In one aspect, the present disclosure provides a method of producing an organic compound, involving (a) culturing a population of host cells in an aqueous culture medium in a bioreactor, wherein the host cells produce the organic compound, (b) introducing into the bioreactor a water-immiscible solvent, wherein the organic compound partitions into the water-immiscible solvent, (c) forming a mixture of the aqueous culture medium and the water-immiscible solvent, (d) selecting a portion of the Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT mixture, (e) separating a plurality of the host cells from the portion of the mixture selected in (d), (f) returning the plurality of the host cells to the bioreactor, and (g) recovering the organic compound from the portion of the mixture selected in (d). In an embodiment, introducing the water-immiscible solvent occurs once during the culturing of the host cells. In another embodiment, introducing the water-immiscible solvent occurs multiple times during the culturing of the host cells. In a further embodiment, introducing the water-immiscible solvent occurs during the culturing of the host cells at a frequency selected from once daily, twice daily, three times daily, four times daily, five times daily, six times daily, seven times daily, eight times daily, nine times daily, ten times daily, eleven times daily, and twelve times daily. In one embodiment, introducing the water-immiscible solvent occurs continuously during culturing of the host cells. In another embodiment, introducing the water-immiscible solvent occurs continuously at a rate of between 0.01 to 1.5 liters per liter of mixture per day. In yet another embodiment, introducing the water-immiscible solvent occurs continuously at a rate of between 0.03 to 1.3 liters per liter of mixture per day. In a further embodiment, introducing the water-immiscible solvent occurs continuously at a rate of between 0.05 to 1.0 liters per liter of mixture per day. In another embodiment, introducing the water-immiscible solvent occurs continuously at a rate of between 0.06 to 0.9 liters per liter of mixture per day. In an embodiment, the organic compound is susceptible to chemical modification in the aqueous culture medium. In another embodiment, the organic compound is inhibitory to the host cells. In another embodiment, the organic compound is a terpene. In some embodiments, the terpene is a C5-C40 terpene. In some embodiments, the terpene is a C5-C20 terpene. In some embodiments, the terpene is a C10-C15 terpene. In another embodiment, the terpene is a hemiterpene, monoterpene, sesquiterpene, diterpene, sesterterpene, triterpene, tetraterpene, or polyterpene. In a further embodiment, the terpene is a monoterpene. In some embodiments, the organic compound is an isoprenoid. In some embodiments, the isoprenoid is a C5-C20 isoprenoid. In some embodiments, the isoprenoid is a C10-C15 isoprenoid. In some embodiments, the isoprenoid is a hemiterpenoid, monoterpenoid, sesquiterpenoid, diterpenoid, sesterterpenoid, triterpenoid, tetraterpenoid, or polyterpenoid. In some embodiments, the isoprenoid is a monoterpenoid. In some embodiments, the organic compound is abietadiene, anethole, amorphadiene, carene, carvacrol, creosol, cuminaldehyde, eugenol, α-farnesene, β-farnesene, farnesol, geranial, geraniol, geranylgeraniol, hinokitiol, isoprene, isoprenol, linalool, limonene, myrcene, nerolidol, ocimene, patchoulol, perillyl alcohol, α-pinene, β-pinene, sabinene, γ-terpinene, terpinolene, thujone, menthol, neral, nerol, eucalyptol, citronellol, citronellal, carvone, isopulegol, valencene, or salvinorin. In some embodiments, the organic compound is β-farnesene. In some embodiments, the organic compound is myrcene. In some embodiments, the organic compound is pinene. In some embodiments, the organic compound is limonene. In some embodiments, the organic compound is menthol. In some embodiments, the organic compound is citronellal. In some embodiments, the organic compound is citronellol. In some embodiments, the organic compound is farnesol. In some Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT embodiments, the organic compound is terpinene. In some embodiments, the organic compound is terpinolene. In some embodiments, the organic compound is geraniol. In some embodiments, the organic compound is linalool. In one embodiment, the host cells are selected from the group consisting of a bacterial cell, a fungal cell, an algal cell, an insect cell, and a plant cell. In another embodiment, the host cells are yeast cells. In another embodiment, the yeast cells are Saccharomyces cerevisiae. In an embodiment, the method involves repeating steps (a) through (g) a plurality of times, optionally wherein the method involves repeating steps (a) through (g) continuously or discontinuously. In another embodiment, the method involves repeating steps (b) through (g) a plurality of times, optionally wherein the method involves repeating steps (b) through (g) continuously or discontinuously. In another embodiment, the method involves repeating steps (b) through (e) a plurality of times, optionally wherein the method involves repeating steps (b) through (e) continuously or discontinuously. In an embodiment, separating a plurality of the host cells from the portion of the mixture selected in (d) occurs by way of a gravity separation process. In some embodiments, the gravity separation process comprises cell sedimentation. In some embodiments, the cell sedimentation is achieved using a gravity settling device. In some embodiments, the gravity settling device comprises (i) an inlet tube that is in fluid communication with, and that receives the portion of the mixture from, the bioreactor; (ii) a settling chamber that is in fluid communication with, and that receives the portion of the mixture from, the inlet tube; (iii) an outlet at the bottom of the settling chamber that is in fluid communication with the vessel; and (iv) an outlet at the top of the settling chamber that is in fluid communication with an effluent vessel. In some embodiments, the gravity settling device further comprises an overflow outlet at the top of the inlet tube that is in fluid communication with the effluent vessel, whereby upon introduction into the inlet tube of an excess of the mixture that exceeds the volume of the settling chamber, the excess mixture flows through the overflow outlet and into the effluent vessel. In some embodiments, the settling chamber and the inlet tube are joined at an angle of from about 60oto about 120o(e.g., 60oto 110o, 60oto 90o, 60oto 80o, 60oto 70o, 70oto 120o, 80oto 120o, 90oto 120o, 100oto 120o, or 80oto 110o), optionally wherein the settling chamber and the inlet tube are joined at an angle of 90o. In some embodiments, the settling chamber comprises one or more baffles. In some embodiments, the settling chamber is gradually sloped between the outlet at the top of the settling chamber that is in fluid communication with an effluent vessel and the inlet tube. In some embodiments, the slope between the outlet at the top of the settling chamber that is in fluid communication with an effluent vessel and the inlet tube is constant. In some embodiments, the slope between the outlet at the top of the settling chamber that is in fluid communication with an effluent vessel and the inlet tube is variable. In some embodiments, the settling chamber is gradually sloped between the outlet at the bottom of the settling chamber that is in fluid communication with the bioreactor and the inlet tube. In some embodiments, the slope between the outlet at the bottom of the settling chamber that is in fluid communication with the bioreactor and the inlet tube is constant. In some embodiments, the slope Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT between the outlet at the bottom of the settling chamber that is in fluid communication with the bioreactor and the inlet tube is variable. In some embodiments, the settling chamber comprises a cone comprising the outlet at the top of the settling chamber that is in fluid communication with the effluent vessel and an inverted cone comprising the outlet at the bottom of the settling chamber that is in fluid communication with the bioreactor. In some embodiments, the settling chamber further comprises a cylinder between the cone and the inverted cone. In some embodiments, the inlet tube intersects with the settling chamber at the interface of the cone and the inverted cone. In some embodiments, the inlet tube intersects with the settling chamber at the cylinder between the cone and the inverted cone. In some embodiments, the inlet tube and the outer edge of the cone form an angle of greater than 0° and less than, or equal to, 90° , optionally wherein the inlet tube and the outer edge of the cone form an angle of from about 25° to about 75° (e.g., 25° to 65°, 25° to 55°, 25° to 45°, 25° to 35°, 35° to 75°, 45° to 75°, 55° to 75°, 65° to 75°, 35° to 65°, 45° to 55°, or 30° to 60°), optionally wherein the inlet tube and the outer edge of the cone form an angle of from about 35° to about 55° (e.g., 35° to 50°, 35° to 45°, 35° to 40°, 40° to 55°, 45° to 55°, 50° to 55°, or 40° to 50°), optionally wherein the inlet tube and the outer edge of the cone form an angle of about 45°. In some embodiments, the cone has an angle of greater than 0° and less than 90° relative to an axis between the outlet at the bottom of the settling chamber that is in fluid communication with the bioreactor and the outlet at the top of the settling chamber that is in fluid communication with an effluent vessel. In some embodiments, the cone has an angle of greater than 5° and less than 65° (e.g., 5° to 10°, 5° to 15°, 5° to 20°, 5° to 25°, 5° to 50°, 25° to 65°, 25° to 55°, 25° to 45°, 25° to 35°, 35° to 75°, 45° to 75°, 55° to 75°, 65° to 75°, 35° to 65°, 45° to 55°, or 30° to 60°) relative to an axis between the outlet at the bottom of the settling chamber that is in fluid communication with the bioreactor and the outlet at the top of the settling chamber that is in fluid communication with an effluent vessel. In some embodiments, the cone has an angle of greater than 5° and less than 45° (e.g., 5° to 40°, 5° to 35°, 5° to 30°, 5° to 25°, 5° to 20°, 5° to 15°, 5° to 10°, 10° to 45°, 15° to 45°, 20° to 45°, 25° to 45°, 30° to 45°, 35° to 45°, 40° to 45°, 10° to 30°, or 15° to 40°) relative to an axis between the outlet at the bottom of the settling chamber that is in fluid communication with the bioreactor and the outlet at the top of the settling chamber that is in fluid communication with an effluent vessel. In some embodiments, the inlet tube and the outer edge of the inverted cone form an angle of greater than 0° and less than, or equal to, -90°, optionally wherein the inlet tube and the outer edge of the inverted cone form an angle of from about -25° to about -75° (e.g., -25° to -65°, -25° to -55°, -25° to -45°, -25° to -35°, -35° to -75°, -45° to -75°, -55° to -75°, -65° to -75°, -35° to -55°, or -40 to -60°), optionally wherein the inlet tube and the outer edge of the inverted cone form an angle of from about - 35° to about -55° (e.g., -35° to -50°, -35° to -45°, -35° to -40°, -40° to -55°, -45° to -55°, or -40° to - 45°), optionally wherein the inlet tube and the outer edge of the inverted cone form an angle of about - 45°. In some embodiments, the inverted cone has an angle of greater than 0° and less than 90° relative to an axis between the outlet at the bottom of the settling chamber that is in fluid communication with the bioreactor and the outlet at the top of the settling chamber that is in fluid communication with an effluent vessel. In some embodiments, the inverted cone has an angle of Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT greater than 5° and less than 65° (e.g., 25° to 65°, 25° to 55°, 25° to 45°, 25° to 35°, 35° to 75°, 45° to 75°, 55° to 75°, 65° to 75°, 35° to 65°, 45° to 55°, or 30° to 60°) relative to an axis between the outlet at the bottom of the settling chamber that is in fluid communication with the bioreactor and the outlet at the top of the settling chamber that is in fluid communication with an effluent vessel. In some embodiments, the inverted cone has an angle of greater than 5° and less than 45° (e.g., 5° to 40°, 5° to 35°, 5° to 30°, 5° to 25°, 5° to 20°, 5° to 15°, 5° to 10°, 10° to 45°, 15° to 45°, 20° to 45°, 25° to 45°, 30° to 45°, 35° to 45°, 40° to 45°, 10° to 30°, or 15° to 40°) relative to an axis between the outlet at the bottom of the settling chamber that is in fluid communication with the bioreactor and the outlet at the top of the settling chamber that is in fluid communication with an effluent vessel. In some embodiments, the inlet tube is connected to the settling chamber by way of a cone. In some embodiments, the cone has an angle of greater than 0° and less than 90° relative to an axis between inlet tube and the settling chamber. In some embodiments, the cone has an angle of greater than 5° and less than 65° (e.g., 25° to 65°, 25° to 55°, 25° to 45°, 25° to 35°, 35° to 75°, 45° to 75°, 55° to 75°, 65° to 75°, 35° to 65°, 45° to 55°, or 30° to 60°) relative to an axis between inlet tube and the settling chamber. In some embodiments, the cone has an angle of greater than 5° and less than 45° (e.g., 5° to 40°, 5° to 35°, 5° to 30°, 5° to 25°, 5° to 20°, 5° to 15°, 5° to 10°, 10° to 45°, 15° to 45°, 20° to 45°, 25° to 45°, 30° to 45°, 35° to 45°, 40° to 45°, 10° to 30°, or 15° to 40°) relative to an axis between inlet tube and the settling chamber. In some embodiments, the cone connecting the inlet tube to the settling chamber is perpendicular to the settling chamber. In some embodiments, the cell sedimentation comprises (i) introducing the portion of the mixture into the inlet tube; (ii) allowing the plurality of the host cells to flow to the bottom of the settling chamber and, subsequently, to return to the bioreactor through the outlet at the bottom of the settling chamber; and (iii) removing the water-immiscible solvent from the settling chamber through the outlet at the top of the settling chamber and delivering the water-immiscible solvent to the effluent bottle. In some embodiments, the portion of the mixture is delivered to the inlet tube by way of a pump. In some embodiments, the water-immiscible solvent is removed from the settling chamber and delivered through the outlet at the top of the settling chamber to the effluent bottle by way of a pump. In some embodiments, the settling chamber is between 0.1 L and 50 L (e.g., 0.1 L and 40 L, 0.1 L and 30 L, 0.1 L and 20 L, 0.1 L and 10 L, 0.1 L and 1 L, 1 L and 50 L, 10 L and 50 L, 20 L and 50 L, 30 L and 50 L, 40 L and 50 L, 20 L and 40 L, 10 L and 30 L, 30 L and 40 L, 10 L and 40 L, 20 L to 40 L, 1 L to 10 L, 1 L to 30 L, 1 L to 20 L, or 5 L to 40 L). In some embodiments, the settling chamber is from 1.5 L to 3 L (e.g., 1.5±0.5 L, 2.0±0.5 L, 2.5±0.5 L, or 3.0±0.5 L). In some embodiments, the settling chamber is greater than 20 L. In some embodiments, the settling chamber is from 20 L to 50 L (e.g., 20 L to 45 L, 20 L to 40 L, 20 L to 35 L, 20 L to 30 L, 20 L to 25 L, 25 L to 50 L, 30 L to 50 L, 35 L to 50 L, 40 L to 50 L, 45 L to 50 L, 30 L to 40 L, 25 L to 35 L, or 35 L to 45 L). In some embodiments, the settling chamber is between 0.1 L and 10 L (e.g., 0.1 L and 8 L, 0.1 L and 6 L, 0.1 L and 4 L, 0.1 L and 2 L, 0.1 L and 1 L, 1 L and 10 L, 2 L and 10 L, 4 L and 10 L, 6 L and 10 L, 8 L and 10 L, 2 L and 6 L) In some embodiments, the bioreactor is between 0.1 L and 1000 L (e.g., 0.1 L and 800 L, 0.1 L and 600 L, 0.1 L and 400 L, 0.1 L and 200 L, 0.1 L and 50 L, 0.1 L and 10 L, 0.1 L and 1 L, 1 L to Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT 100 L, 10 L and 500 L, 0.1 L and 50 L, 10 L and 100 L, 50 L and 1000 L, 200 L and 1000 L, 400 L and 1000 L, 600 L and 1000 L, 800 L and 1000 L, 400 L and 800 L, 200 L and 500 L, 500 L and 700 L, 300 L and 600 L). In some embodiments, the bioreactor is greater than 200 L. In some embodiments, the bioreactor is between 0.1 L and 100 L (e.g., 0.1 L and 80 L, 0.1 L and 60 L, 0.1 L and 40 L, 0.1 L and 20 L, 0.1 L and 1 L, 1 L and 100 L, 20 L and 100 L, 40 L and 100 L, 60 L and 100 L, 80 L and 100 L, or 1 L and 50 L). In some embodiments, the bioreactor is between 0.1 L and 10 L (e.g., 0.1 L and 8 L, 0.1 L and 6 L, 0.1 L and 4 L, 0.1 L and 2 L, 0.1 L and 1 L, 1 L and 10 L, 2 L and 10 L, 4 L and 10 L, 6 L and 10 L, 8 L and 10 L, 2 L and 6 L). In some embodiments, the bioreactor is between 200 L and 1000 L (e.g., 200 L and 800 L, 200 L and 600 L, 200 L and 400 L, 200 L and 300 L, 300 L and 1000 L, 500 L and 1000 L, 600 L and 1000 L, 800 L and 1000 L, or 400 L and 800 L). In an embodiment, the method results in performance enhancement of the host cells relative to a reference method which does not involve steps (b) through (g). In another embodiment, the method results in a performance enhancement of the host cells from about 0.5% to about 500% (e.g., 0.5% to 400%, 0.5% to 300%, 0.5% to 200%, 0.5% to 100%, 0.5% to 50%, 50% to 500%, 100% to 500%, 200% to 500%, 300% to 500%, 400% to 500%, 10% to 100%, 10% to 200%, 100% to 300%, or 50% to 200%) relative to a reference method which does not involve steps (b) through (g). In yet another embodiment, the method results in an increase in yield of the organic compound relative to a reference method which does not involve steps (b) through (g). In a further embodiment, the method results in an increase in yield of the organic compound from about 0.5% to about 500% (e.g., 0.5% to 400%, 0.5% to 300%, 0.5% to 200%, 0.5% to 100%, 0.5% to 50%, 50% to 500%, 100% to 500%, 200% to 500%, 300% to 500%, 400% to 500%, 10% to 100%, 10% to 200%, 100% to 300%, or 50% to 200%) relative to a reference method which does not involve steps (b) through (g). In yet another embodiment, the method results in an increase in productivity of the organic compound relative to a reference method which does not involve steps (b) through (g). In another embodiment, the method results in an increase in productivity of the organic compound from about 0.5% to about 500% (e.g., 0.5% to 400%, 0.5% to 300%, 0.5% to 200%, 0.5% to 100%, 0.5% to 50%, 50% to 500%, 100% to 500%, 200% to 500%, 300% to 500%, 400% to 500%, 10% to 100%, 10% to 200%, 100% to 300%, or 50% to 200%) relative to a reference method which does not involve steps (b) through (g). In some embodiments, the host cells in the aqueous culture medium in the bioreactor consume oxygen at a rate of from about 25 mmol / L / hr to about 250 mmol / L / hr (e.g., 25 mmol / L / hr to 200 mmol / L / hr, 25 mmol / L / hr to 150 mmol / L / hr, 25 mmol / L / hr to 100 mmol / L / hr, 25 mmol / L / hr to 75 mmol / L / hr, 25 mmol / L / hr to 50 mmol / L / hr, 50 mmol / L / hr to 250 mmol / L / hr, 100 mmol / L / hr to 250 mmol / L / hr, 150 mmol / L / hr to 250 mmol / L / hr, 200 mmol / L / hr to 250 mmol / L / hr, 100 mmol / L / hr to 200 mmol / L / hr, 75 mmol / L / hr to 150 mmol / L / hr, or 100 mmol / L / hr to 150 mmol / L / hr). In some embodiments, the host cells in the aqueous culture medium in the bioreactor consume oxygen at a rate of from about 90 mmol / L / hr to about 130 mmol / L / hr (e.g., 90 mmol / L / hr to 120 mmol / L / hr, 90 mmol / L / hr to 110 mmol / L / hr, 90 mmol / L / hr to 100 mmol / L / hr, 100 mmol / L / hr to 130 mmol / L / hr, 110 mmol / L / hr to 130 mmol / L / hr, 120 mmol / L / hr to 130 mmol / L / hr, 100 mmol / L / hr to 120 mmol / L / hr, or 100 mmol / L / hr to 110 mmol / L / hr). In some embodiments, the host cells in the aqueous culture medium in the bioreactor consume oxygen at a rate of from about 110 mmol / L / hr. In some embodiments, the Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT water-immiscible solvent is added to the bioreactor at a rate of from about 0.05 L / L / day to about 1 L / L / day (e.g., 0.05 L / L / day to 0.8 L / L / day, 0.05 L / L / day to 0.6 L / L / day, 0.05 L / L / day to 0.4 L / L / day, 0.05 L / L / day to 0.2 L / L / day, 0.05 L / L / day to 0.1 L / L / day, 0.1 L / L / day to 1 L / L / day, 0.2 L / L / day to 1 L / L / day, 0.4 L / L / day to 1 L / L / day, 0.6 L / L / day to 1 L / L / day, 0.8 L / L / day to 1 L / L / day, 0.2 L / L / day to 0.6 L / L / day, or 0.4 L / L / day to 0.8 L / L / day). In some embodiments, the water-immiscible solvent is added to the bioreactor at a rate of from about 0.2 L / L / day to about 0.6 L / L / day (e.g., 0.2 L / L / day to 0.5 L / L / day, 0.2 L / L / day to 0.4 L / L / day, 0.2 L / L / day to 0.3 L / L / day, 0.3 to 0.6 L / L / day, 0.4 L / L / day to 0.6 L / L / day, 0.5 L / L / day to 0.6 L / L / day, or 0.3 L / L / day to 0.5 L / L / day). In one aspect, the present disclosure provides an organic compound produced using the method of any one of the preceding paragraphs. In an embodiment, the organic compound is a terpene. In some embodiments, the terpene is a C5-C40 terpene. In some embodiments, the terpene is a C5-C20 terpene. In some embodiments, the terpene is a C10-C15 terpene. In another embodiment, the terpene is a hemiterpene, monoterpene, sesquiterpene, diterpene, sesterterpene, triterpene, tetraterpene, or polyterpene. In another embodiment, the terpene is a monoterpene. In some embodiments, the organic compound is an isoprenoid. In some embodiments, the isoprenoid is a C5-C20 isoprenoid. In some embodiments, the isoprenoid is a C10-C15 isoprenoid. In some embodiments, the isoprenoid is a hemiterpenoid, monoterpenoid, sesquiterpenoid, diterpenoid, sesterterpenoid, triterpenoid, tetraterpenoid, or polyterpenoid. In some embodiments, the isoprenoid is a monoterpenoid. In some embodiments, the organic compound is abietadiene, anethole, amorphadiene, carene, carvacrol, creosol, cuminaldehyde, eugenol, α-farnesene, β-farnesene, farnesol, geranial, geraniol, geranylgeraniol, hinokitiol, isoprene, isoprenol, linalool, limonene, myrcene, nerolidol, ocimene, patchoulol, perillyl alcohol, α-pinene, β-pinene, sabinene, γ-terpinene, terpinolene, thujone, menthol, neral, nerol, eucalyptol, citronellol, citronellal, carvone, isopulegol, valencene, or salvinorin. In some embodiments, the organic compound is β-farnesene. In some embodiments, the organic compound is myrcene. In some embodiments, the organic compound is pinene. In some embodiments, the organic compound is limonene. In some embodiments, the organic compound is menthol. In some embodiments, the organic compound is citronellal. In some embodiments, the organic compound is citronellol. In some embodiments, the organic compound is farnesol. In some embodiments, the organic compound is terpinene. In some embodiments, the organic compound is terpinolene. In some embodiments, the organic compound is geraniol. In some embodiments, the organic compound is linalool. BRIEF DESCRIPTION OF THE DRAWINGS FIG.1 depicts an exemplary glass tube separation device for in-situ product removal (ISPR) in a 0.5 L fermentor (MF = main fermentor). FIG.2 depicts an alternative glass tube separation device for in-situ product removal (MF = main fermentor). FIG.3 depicts an exemplary lab scale standard (non-ISPR) fermentation plot of oxygen uptake rate (OUR) over time. Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT FIG.4A and FIG.4B depict the OUR of a standard (non-ISPR) fed batch process compared to a bolus process (ISPR V1) (FIG.4A), and myrcene titer (g / kg) over time (hr) (FIG.4B) in a 0.5 L fermentation tank (exclusive of effluent bottle). FIG.5A and FIG.5B depict yield (FIG.5A) and productivity (FIG.5B) for a standard (non- ISPR) fed batch process compared to a bolus process (ISPR V1). FIG.6 depicts an OUR vs. time plot in a 0.5 L fermentation tank. “Bolus” refers to ISPR V1 and “Continuous” refers to ISPR V2. FIG.7A and FIG.7B depict yield (FIG.7A) and productivity (FIG.7B) for Bolus (ISPR V1) and Continuous (ISPR V2). FIG.8A and FIG.8B depict yield (FIG.8A) and productivity (FIG.8B) based on overlay perfusion rates in a continuous (ISPR V2) process. FIG.9 depicts an exemplary vertical delta separation device (VDS) for in-situ product removal in a lab scale fermentor (MF = main fermentor). FIG.10 depicts % overlay in the effluent collected every 24 hours starting on day 2 of the fermentation until day 7. The shaded area represents regions of % overlay from historical runs with a glass tube separation device under different overlay perfusion rates. The solid line represents a reverse glass tube separation device used as a control in the present experiment. The dashed line represents the VDS separation device. FIG.11A and FIG.11B depict cumulative yield (FIG.11A) and productivity (FIG.11B) of a reverse separation device, VDS, and non-ISPR run. FIG.12 depicts a schematic of the 20 L ISPR fermentation setup with settling unit. FIG.13A and FIG.13B depicts a schematic of the 300 L ISPR fermentation setup with settling unit (FIG.13A) which may use a VDS (FIG.13B). FIG.14A and FIG.14B show the separation of fractions of from the whole cell broth (FIG. 14A) and effluent stream (FIG.14B) when fermentation was performed at 20 L scale using a 1.5 L settler. FIG.15A and FIG.15B show a comparison of product yield (%) (FIG.15A) and volumetric productivity (g / L / h) (FIG.15B) for fermentation performed at a scale of 2 L and 20 L. FIG.16A and FIG 16B show the separation of fractions of from the whole cell broth (FIG. 16A) and effluent stream (FIG.16B) when fermentation was performed at 300 L scale using a 24 L settler. FIG.17A and FIG.17B show a comparison of product yield (%) (FIG.17A) and volumetric productivity (g / L / h) (FIG.17B) for fermentation performed at a scale of 2 L and 300 L. FIG.18 shows the separation of overlay fractions of from the whole cell broth when fermentation was performed at 300 L scale using a VDS. FIG.19 shows the separation of overlay fractions of from the effluent stream when fermentation was performed at 300 L scale using a VDS. FIG.20A and FIG.20B show a comparison of product yield (%) (FIG.20A) and volumetric productivity (g / L / h) (FIG.20B) for fermentation performed at a scale of 2 L, 300 L with a commercial settler, and 300 L with a VDS. Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT FIG.21A – FIG.21D show a comparison of linalool product yield (%) (FIG.21A), volumetric productivity (g / L / h) (FIG.21B), total linalool produced (g) (FIG.21C), and relative percent improvement of ISPR over the batch process (FIG.21D) for fermentations performed using a batch process with 10% EsterexTMA32 and fermentations performed using ISPR with EsterexTMA32. FIG.22A – FIG.22D show a comparison of linalool product yield (%) (FIG.22A), volumetric productivity (g / L / h) (FIG.22B), total linalool produced (g) (FIG.22C), and relative percent improvement (FIG.22D) for fermentations performed using a ISPR with 10% DrakeolTM10 and fermentations performed using ISPR with EsterexTMA32. DETAILED DESCRIPTION OF THE EMBODIMENTS Definitions As used herein, 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 “aqueous culture medium” refers to a medium that is suitable for culturing cells which uses water as the water-based medium. As used herein in the context of extracting a cell culture product (e.g., a hydrophobic, lipophilic, and / or nonpolar cell culture product, such as a hydrophobic, lipophilic, and / or nonpolar fermentation product) present within a cell culture composition into an added solvent (e.g., a water- immiscible solvent described herein), the cell culture product is considered to be “partitioned between” the cell culture composition and the added solvent when the cell culture product reaches a distribution among the cell culture composition component and the added solvent component. The cell culture product may, for example, distribute such that the majority of the cell culture product is found within the added solvent (e.g., as in the case of a hydrophobic, lipophilic, or nonpolar cell culture product and a water-immiscible solvent). In some embodiments, the cell culture product distributes such that essentially all of the cell culture product is found within the added solvent. The cell culture product may be allowed, for example, to establish a dynamic equilibrium between the cell culture composition and the added solvent, such that the equilibrium concentration of the cell culture product within each component is reflective of the partition coefficient for the cell culture product and the mixture formed by the cell culture composition and added solvent. In some embodiments, the cell culture product is continuously extracted by the added solvent (e.g., through the use of fresh, added solvent), such that the majority (or essentially all) of the cell culture product is consistently found within the added solvent. In alternative embodiments, the cell culture product is discontinuously extracted by the added solvent (e.g., in a series of discrete extraction steps). Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT As used herein, the term “baffle” refers to an object within a vessel or the side of a vessel which increases the surface area of the vessel. As used herein, the term “capable of producing” refers to a host cell which is genetically modified to include 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) “capable of producing” an isoprenoid is one that contains the enzymes necessary for production of the isoprenoid according to the isoprenoid biosynthetic pathway. As used herein, the term “cell sedimentation” refers to a process of separating a portion of cells from one or more other components of a composition over time wherein cells migrate toward a bottom surface of a vessel, e.g., by gravity. In some embodiments of the disclosure, cell sedimentation can be used to collect cells, e.g., from the cell culture composition, and recycle cells back to the cell culture mixture in order to maintain biomass. Therefore, cell sedimentation does not require cells to permanently settle at the bottom surface of a vessel. As used herein, the term “cell culture product” refers to a compound that is produced by a host cell (e.g., yeast cell, bacteria cell, fungi cell, plant cell, or animal cell), which is cultured in a medium and under conditions suitable for the host cells to produce the cell culture product. The cell culture product may be naturally produced by the host cells or may be produced by host cells that have been genetically modified to produce the cell culture product. An example of a cell culture product is an isoprenoid or a terpene. In some embodiments, the cell culture product may be a fermentation product which refers to a cell culture product that is produced through a fermentation process, wherein the host cell is, for example, a yeast cell. In some embodiment, the cell culture product may be produced by a host cell that is a bacteria cell. Examples of host cells that may be used to produce a cell culture product are described below in the section titled Host Cell Strains. As used herein, the term “cell culture composition” refers to a composition which contains host cells (e.g., yeast cells, bacteria cells, fungi cells, plant cells, or animal cells), and products or metabolites produced by the host cells, which may be genetically modified. An example of a cell culture composition is a whole cell broth, which may be the entire contents of a vessel, including cells, aqueous-phase culture medium, and compounds produced from the genetically modified host cells. In some embodiments, a cell culture composition of the disclosure may be contacted with a water- immiscible solvent. In some embodiments, the cell culture composition is a fermentation composition, wherein the fermentation composition contains yeast cells and products or metabolites produced by the yeast cells, which may be genetically modified. Examples of host cells that may be part of cell culture composition are described below in the section titled Host Cell Strains. As used herein, the term “cone” refers to a geometric shape which gradually expands from a first point or plane to a second plane, wherein the expansion of the cone may be constant or may be variable. For example, a device or system in which cell sedimentation occurs may include one or more cones. As used herein, “chemical modification” refers to changes to a chemical’s structure and / or formula, including but not limited to changes caused by degradation and oxidation. Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT 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 cell culture composition which contains fermented host cells, for example yeast cells, and products or metabolites produced by the fermented host cells, which may be genetically modified. An example of a fermentation composition is a whole cell broth, which may be the entire contents of a vessel, including fermented host cells, aqueous-phase culture medium, and compounds produced from the genetically modified host cells. In some embodiments, a fermentation composition of the disclosure may be contacted with a water- immiscible solvent. 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 refer to a set of at least one coding sequence, where the coding sequence encodes an enzyme that catalyzes different parts of a synthetic pathway to form a desired product (e.g., cell culture product, e.g., an isoprenoid or a terpene, among others). 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 2 or more members (e.g., 2, 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 “gravity separation” refers to a process of separating two or more compositions from one another using gravity, optionally in addition to using gravity in the context of a gravity enhancing means, such as a centrifuge, hydrocyclone, or membrane. Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT As used herein, the term "heterologous" refers to what is not normally found in nature. The term "heterologous compound" refers to the production of a compound by a cell that does not normally produce the compound, or to the production of a compound at a level not normally produced by the cell. For example, a cell culture product (e.g., an isoprenoid or a terpene, among others) can be a heterologous compound. 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 invention refers to a microorganism, such as yeast, and includes an individual cell or cell culture contains 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. As used herein, the term “inhibitory” or “inhibitory effect” refers to negatively impacting cell health, including, but not limited to, growth, maintenance, and replication, or productivity. As used herein, the term “medium” refers to a culture medium or a fermentation medium. A medium may be a mixture. As used herein, the term “mixture” means a composition made of two or more different substances that are mixed. In some cases, a mixture described herein can be a homogenous mixture of the two or more different substances, e.g., the mixture can have the same proportions of its components (e.g., the two or more substances) throughout any given sample of the mixture. In some cases, a mixture as provided herein can be a heterogeneous mixture of the two or more different substances, e.g., the proportions of the components of the mixture (e.g., the two or more substances) can vary throughout the mixture. In some cases, a mixture is a liquid solution, e.g., the mixture is present in liquid phase. In some instances, a liquid solution can be regarded as comprising a liquid solvent and a solute. Mixing a solute in a liquid solvent can be termed as “dissolution” process. In some cases, there is more than one solvent and / or more than one solute. In some cases, a mixture is a colloid, liquid suspension, emulsion, or multiphasic. As used herein, the terms “oil,” “overlay oil,” or “overlay” refer to a biologically compatible hydrophobic, lipophilic, substance including but not limited to geologically-derived crude oil, distillate fractions of geologically-derived crude oil, vegetable oil, algal oil, microbial lipids, mineral oil, synthetic oils, or a derivative thereof. The oil is neither itself inhibitory to a biological molecule, a cell, a tissue, or a subject, nor does it degrade (if the oil degrades) at a rate that produces byproducts at inhibitory concentrations to a biological molecule, a cell, a tissue, or a subject. Preferred examples of oils include but are not limited to avocado oil, canola oil, grapeseed oil, hemp oil, soybean oil, jojoba oil, mineral oil, and sunflower oil. The term “performance enhancement” refers to relative performance increase as defined as the ratio of the performance of the culture implementing the claimed methods to the performance of the culture without the claimed methods. Culture performance parameters could include yield, Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT productivity, or length or duration of culture. The range of performance enhancement could be, for example, from 0.5% to 500% of the performance of the culture without the claimed methods. As used herein, the terms “polypeptide,” “peptide,” and “protein” are used interchangeably to refer to a polymer of amino acid residues. The terms encompass amino acid chains of any length, including full-length proteins, wherein the amino acid residues are linked by covalent peptide bonds. As used herein, the term "productivity" refers to production of a compound by a cell, expressed as the amount of compound produced (by weight) per amount of culture medium in which the cell is cultured (by volume) over time (per hour). As used herein, the term "production" generally refers to an amount of compound produced by a genetically modified host cell provided herein. In some embodiments, production is expressed as a yield of the compound by 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 “water-immiscible solvent” refers to a solvent which does not form a homogenous mixture when added to water. A water-immiscible solvent may be an overlay. A water- immiscible solvent may be an alcohol (e.g., a C10-C20 alcohol). In some embodiments, the water- immiscible solvent is DRAKEOL 10. In other embodiments, the water-immiscible solvent is DURASYN 164. In other embodiments, the water-immiscible solvent is JARCOL-16. In some embodiments the water-immiscible solvent ESTEREX A32. In some embodiments, the water- immiscible solvent is an oil. The water-immiscible solvent may also be, for example, corn oil, sunflower oil, soybean oil, mineral oil, polyalphaolefin, dodecane, hexadecane, oleyl alcohol, butyl oleate, dibutyl phthalate, dodecanol, dioctyl phthalate, farnesene, or isopropyl myristate. As used herein, the term "yield" refers to production of a compound by a cell, expressed as the amount of compound produced per amount of carbon source consumed by the cell, by weight. Enhanced Cell Culture Performance and Product Recovery In one aspect, the present disclosure provides a method of producing an organic compound comprising: (a) culturing a population of host cells in an aqueous culture medium in a bioreactor, wherein the host cells produce the organic compound, (b) introducing into the bioreactor a water- immiscible solvent, wherein the organic compound partitions into the water-immiscible solvent, (c) forming a mixture of the aqueous culture medium and the water-immiscible solvent, (d) selecting a portion of the mixture, (e) separating a plurality of the host cells from the portion of the mixture selected in (d), (f) returning the plurality of the host cells to the bioreactor, and (g) recovering the organic compound from the portion of the mixture selected in (d). In one embodiment, introducing the water-immiscible solvent occurs once during the culturing of the host cells. In another embodiment, introducing the water-immiscible solvent occurs multiple times during the culturing of the host cells. In another embodiment, introducing the water-immiscible solvent occurs during the culturing of the host cells at a frequency selected from once daily, twice daily, three times daily, four times daily, five times daily, six times daily, seven times daily, eight times daily, nine times daily, ten times daily, eleven times daily, and twelve times daily. Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT In an embodiment, introducing the water-immiscible solvent occurs continuously during culturing of the host cells. In a further embodiment, introducing the water-immiscible solvent occurs continuously at a rate of between 0.01 to 1.5 liters per liter of mixture per day. In a further embodiment, introducing the water-immiscible solvent occurs continuously at a rate of between 0.03 to 1.3 liters per liter of mixture per day. In yet another embodiment, introducing the water-immiscible solvent occurs continuously at a rate of between 0.05 to 1.0 liters per liter of mixture per day. In yet another embodiment, introducing the water-immiscible solvent occurs continuously at a rate of between 0.06 to 0.9 liters per liter of mixture per day. In one embodiment, the organic compound is susceptible to chemical modification in the aqueous culture medium. In one embodiment, the organic compound is inhibitory to the host cells. In another embodiment, the organic compound is a terpene. The terpene may be a C5-C40 terpene. In some embodiments, the terpene is a C5-C20 terpene. In some embodiments, the terpene is a C10-C15 terpene. In another embodiment, the terpene is a hemiterpene, monoterpene, sesquiterpene, diterpene, sesterterpene, triterpene, tetraterpene, or polyterpene. In yet another embodiment, the terpene is a monoterpene. In some embodiments, the organic compound is an isoprenoid. In some embodiments, the isoprenoid is a C5-C20 isoprenoid. In some embodiments, the isoprenoid is a C10-C15 isoprenoid. In some embodiments, the isoprenoid is a hemiterpenoid, monoterpenoid, sesquiterpenoid, diterpenoid, sesterterpenoid, triterpenoid, tetraterpenoid, or polyterpenoid. In some embodiments, the isoprenoid is a monoterpenoid. In some embodiments, the organic compound is abietadiene, anethole, amorphadiene, carene, carvacrol, creosol, cuminaldehyde, eugenol, α-farnesene, β-farnesene, farnesol, geranial, geraniol, geranylgeraniol, hinokitiol, isoprene, isoprenol, linalool, limonene, myrcene, nerolidol, ocimene, patchoulol, perillyl alcohol, α-pinene, β-pinene, sabinene, γ-terpinene, terpinolene, thujone, menthol, neral, nerol, eucalyptol, citronellol, citronellal, carvone, isopulegol, valencene, or salvinorin. In some embodiments, the organic compound is β-farnesene. In some embodiments, the organic compound is myrcene. In some embodiments, the organic compound is pinene. In some embodiments, the organic compound is limonene. In some embodiments, the organic compound is menthol. In some embodiments, the organic compound is citronellal. In some embodiments, the organic compound is citronellol. In some embodiments, the organic compound is farnesol. In some embodiments, the organic compound is terpinene. In some embodiments, the organic compound is terpinolene. In some embodiments, the organic compound is geraniol. In some embodiments, the organic compound is linalool In an embodiment, the host cells are selected from the group consisting of a bacterial cell, a fungal cell, an algal cell, an insect cell, and a plant cell. In an embodiment, the host cells are yeast cells. In an embodiment, the yeast cells are Saccharomyces cerevisiae. In one embodiment, the method further comprises repeating steps (a) through (g) a plurality of times, optionally wherein the method comprises repeating steps (a) through (g) continuously or discontinuously. In another embodiment, the method further comprises repeating steps (b) through Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT (g) a plurality of times, optionally wherein the method comprises repeating steps (b) through (g) continuously or discontinuously. In a further embodiment, the method further comprises repeating steps (b) through (e) a plurality of times, optionally wherein the method comprises repeating steps (b) through (e) continuously or discontinuously. In an embodiment, separating a plurality of the host cells from the portion of the mixture selected in (d) occurs by way of a gravity separation process. In an embodiment, the method results in performance enhancement of the host cells relative to a reference method which does not comprise steps (b) through (g). In an embodiment, the method results in a performance enhancement of the host cells of from about 0.5% to about 500% relative to a reference method which does not comprise steps (b) through (g). In another embodiment, the method results in an increase in yield of the organic compound relative to a reference method which does not comprise steps (b) through (g). In another embodiment, the method results in an increase in yield of the organic compound from about 0.5% to about 500% relative to a reference method which does not comprise steps (b) through (g). In yet another embodiment, the method results in an increase in productivity of the organic compound relative to a reference method which does not comprise steps (b) through (g). In a further embodiment, the method results in an increase in productivity of the organic compound from about 0.5% to about 500% relative to a reference method which does not comprise steps (b) through (g). In one aspect, the present disclosure provides an organic compound produced using the method of any one of the preceding paragraphs. In an embodiment, the organic compound is a terpene. In an embodiment, the terpene is a hemiterpene, monoterpene, sesquiterpene, diterpene, sesterterpene, triterpene, tetraterpene, or polyterpene. In another embodiment, the terpene is a monoterpene. In yet another embodiment, the monoterpene is limonene, citranellol, geraniol, menthol, perillyl alcohol, linalool, thujone, myrcene, hinokitiol, carvacrol, anethole, cuminaldehyde, eucalyptol, α-pinene, β-pinene, citronellal, isopulegol, nerol, neral, geranial, or carvone. Cell Culture Products Described herein are methods of producing an organic compound as the product of cell culture, as well as methods of isolating an organic compound from a cell culture medium. In some embodiments, the organic compound is a water-immiscible compound. For example, the organic compound may have a log(D) value of from about 1 to about 15, or the water-immiscible may have a log(Kd) value of from about 1 to about 15, where Kd is the partition coefficient for the product between the water-immiscible solvent and the culture medium. In some embodiments, the organic compound is a compound that is inhibitory to the host cells and / or is susceptible to chemical modification in the cell culture medium. As discussed above, some compounds of interest are inhibitory to the host cells such that as the host cells produce the organic compound in the culture medium, accumulation of the organic compound decreases host cell health. Examples of organic compounds include isoprenoids and terpenes, among others known in the art and described herein. Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT Isoprenoids In some embodiments, the organic compound is an isoprenoid. The isoprenoid may be a C5- C40 isoprenoid (e.g., a C5 isoprenoid, C10 isoprenoid, C15 isoprenoid, C20 isoprenoid, C25 isoprenoid, C30 isoprenoid, C35 isoprenoid, or C40 isoprenoid). For example, in some embodiments, the isoprenoid is a C20 isoprenoid. These compounds are derived from four isoprene units and also called diterpenoids. Illustrative examples of diterpenoids are casbene, eleutherobin, paclitaxel, prostratin, pseudopterosin, taxadiene, and salvinorins. In yet other examples, the isoprenoid is a C20+ isoprenoid. These compounds are derived from more than four isoprene units and include: triterpenoids (C30 isoprenoid compounds derived from 6 isoprene units) such as arbrusidee, bruceantin, testosterone, progesterone, cortisone, digitoxin, and squalene; tetraterpenoids (C40 isoprenoid compounds derived from 8 isoprenoids) such as β-carotene; and polyterpenoids (C40+ isoprenoid compounds derived from more than 8 isoprene units) such as polyisoprene. In some embodiments, the isoprenoid is selected from the group consisting of abietadiene, amorphadiene, carene, α-farnesene, β-farnesene, farnesol, geraniol, geranylgeraniol, isoprene, linalool, limonene, myrcene, nerolidol, ocimene, patchoulol, β-pinene, sabinene, y-terpinene, terpinolene, valencene, retinol, phytol, retinal, santalol, santalene, sinensol, squalene, bisabolol, sclareol, eugenol, and creosol. The isoprenoid product may be a C5-C20 isoprenoid (e.g., C5 isoprenoid, C6 isoprenoid, C7 isoprenoid, C8 isoprenoid, C9 isoprenoid, C10 isoprenoid, C11 isoprenoid, C12 isoprenoid, C13 isoprenoid, C14 isoprenoid, C15 isoprenoid, C16 isoprenoid, C17 isoprenoid, C18 isoprenoid, C19 isoprenoid, or C20 isoprenoid). In some embodiments, the isoprenoid produced by the cell is a C5 isoprenoid. These compounds are derived from one isoprene unit and are also called hemiterpenoids. Illustrative examples of a hemiterpenoid are isoprene and isoprenol. The isoprenoid product may be a C10-C15 isoprenoid (e.g., C10 isoprenoid, C11 isoprenoid, C12 isoprenoid, C13 isoprenoid, C14 isoprenoid, or C15 isoprenoid). In other embodiments, the isoprenoid is a C10 isoprenoid. These compounds are derived from two isoprene units and are also called monoterpenoids. Illustrative examples of monoterpenoids are limonene, citranellol, geraniol, menthol, perillyl alcohol, linalool, thujone, myrcene, hinokitiol, carvacrol, anethole, cuminaldehyde, eucalyptol, α-pinene, β-pinene, citronellal, isopulegol, nerol, neral, geranial, and carvone. In other embodiments, the isoprenoid is a C15 isoprenoid. These compounds are derived from three isoprene units and are also called sesquiterpenoids. Illustrative examples of sesquiterpenoids are periplanone B, gingkolide B, amorphadiene, artemisinin, artemisinic acid, valencene, nootkatone, epicedrol, epiaristolochene, farnesol, gossypol, sanonin, periplanone, forskolin, and patchoulol, which is also known as patchouli alcohol. Isoprenoid compounds also include, but are not limited to, carotenoids (such as lycopene, α- and β-carotene, α- and β-cryptoxanthin, bixin, zeaxanthin, astaxanthin, and lutein), steroid compounds, cannabinoids, and compounds that are composed of isoprenoids modified by other chemical groups, such as mixed terpene-alkaloids, and coenzyme Q (CoQ) enzymes, such as, for example, coenzyme Q-10. Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT In some embodiments, the isoprenoid is a hemiterpenoid, monoterpenoid, sesquiterpenoid, diterpenoid, sesterterpenoid, triterpenoid, tetraterpenoid, or polyterpenoid. In some embodiments, the isoprenoid is a monoterpenoid. Terpenes In some embodiments, the product is a terpene. In some embodiments, the terpene is a C5- C40 terpene (e.g., a C5 terpene, C10 terpene, C15 terpene, C20 terpene, C25 terpene, C30 terpene, C35 terpene, or C40 terpene). In some embodiments, the terpene is a C5-C20 terpene (e.g., C5 terpene, C6 terpene, C7 terpene, C8 terpene, C9 terpene, C10 terpene, C11 terpene, C12 terpene, C13 terpene, C14 terpene, C15 terpene, C16 terpene, C17 terpene, C18 terpene, C19 terpene, or C20 terpene). In some embodiments, the terpene is a C10-C15 terpene (e.g., C10 terpene, C11 terpene, C12 terpene, C13 terpene, C14 terpene, or C15 terpene). In some embodiments, the terpene is a hemiterpene, monoterpene, sesquiterpene, diterpene, sesterterpene, triterpene, tetraterpene, or polyterpene. In some embodiments, the terpene is a monoterpene. Monoterpenes are C10 terpenes and are derived from two isoprene units. For example, the monoterpene may be carene, whose structure is: Carene is typically made from GPP by 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) for use as heterologous sequences that encode carene synthase. Another monoterpene, such as geraniol, (also known as rhodnol), whose structure is may be a product produced by the present invention. Geraniol is typically made from OPP by geraniol synthase. Illustrative examples of suitable nucleotide sequences include but are not limited to: (AJ457070; Cinnamomum tenuipilum), (AY362553; Ocimum basilicum), (DQ234300; Perilla frutescens strain 1864), (DQ234299; Perilla citriodora strain 1861), (DQ234298; Perilla citriodora strain 4935), and (DQ088667; Perilla citriodora) for encoding geraniol synthase that may be used a heterologous sequence of the present invention. The monoterpene, linalool, whose structure is: is typically made from GPP by linalool synthase and may be produced by the present invention. Illustrative examples of a suitable nucleotide sequence include, but are not limited to: (AF497485; Arabidopsis thaliana), (AC002294, Locus AAB71482; Arabidopsis thaliana), Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT (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; Perilla frutescens), (AY473623; Picea abies), (DQ195274; Picea sitchensis), and (AF444798; Perilla frutescens var. crispa cultivar No.79). These sequences may be used as heterologous sequences of the present invention. Another monoterpene, limonene whose structure is: is typically made from GPP by limonene synthase. Illustrative examples of suitable nucleotide sequences that may be used as heterologous sequences of the present invention 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 (MC4SLSP, REGION: 29...1828; Mentha spicata). The monoterpene, myrcene, whose structure is: is typically made from GPP by myrcene synthase and is another product that may be produced by the present invention. Illustrative examples of suitable nucleotide sequences that may be used as heterologous sequences of the present invention include but are not limited to: (187908; Abies grandis), (AY195609; Antirrhinum majus), (AY195608; Antirrhinum majus), (NM—127982; Arabidopsis thaliana TPS10), NM—113485; Arabidopsis thaliana ATTPS-CIN), (NM—13483; Arabidopsis thaliana ATIPS-CIN), (AF271259; Perilla frutescens), (AY473626; Picea abies), (AF369919; Picea abies), and (AJ304839; Quercus ilex). Another monoterpene, ocimene, α- and β-Ocimene, whose structures are: respectively, are typically made from GPP by ocimene synthase, a synthase that may be encoded by the heterologous sequences of the present invention. Illustrative examples of suitable nucleotide sequences that may be used as heterologous sequences include but are not limited to: (AY195607; Antirrhinum majus), (AY195609; Antirrhinum majus), (AY195608; Antirrhinum majus), (AK221024; Arabidopsis thaliana), (NM—113485; Arabidopsis thaliana ATTPS-CIN), (NM— Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT 113483; Arabidopsis thaliana ATTPS-CIN), (NM—117775; Arabidopsis thaliana ATTPS03), (NM— 001036574; Arabidopsis thaliana ATTPS03), (NM—127982; Arabidopsis thaliana TPS10), (AB110642; Citrus unshiu CitMTSL4), and (AY575970; Lotus corniculatus var. japonicus). Another monoterpene, α-pinene whose structure is: is typically made from GPP by α-pinene synthase, a synthase that may be encoded by the heterologous sequences of the present invention. Illustrative examples of suitable nucleotide sequences that may be used as heterologous sequences to encode the synthase 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 (+) / (−)α-pinene synthase (AGU87909, REGION: 6111892; Abies grandis). Another monoterpene, β-pinene, whose structure is: is typically made from GPP by β-pinene synthase, a synthase that may be encoded by the heterologous sequences of the present invention. Illustrative examples of suitable nucleotide sequences that may be used as heterologous sequences to encode the synthase include but are not limited to: (−) β-pinene synthases (AF276072, REGION: 1...1749; Artemisia annua) and (AF514288, REGION: 26...1834; Citrus limon). Another monoterpene, sabinene, whose structure is: is typically made from GPP by sabinene synthase, a synthase that may be encoded by the heterologous sequences of the present invention. An illustrative example of a suitable nucleotide sequence that may be used as a heterologous sequence of include but is not limited to AF051901, REGION: 26...1798 from Salvia officinalis. Another monoterpene, γ-terpinene, whose structure is: is typically made from GPP by a γ-terpinene synthase, a synthase that may be encoded by the heterologous sequences of the present invention. Illustrative examples of suitable nucleotide Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT sequences that may be used as heterologous sequences include but are not limited to: (AF514286, REGION: 30...1832 from Citrus limon) and (AB110640, REGION 1…1803 from Citrus unshiu). Another monoterpene, terpinolene, whose structure is is typically made from GPP by terpinolene synthase, a synthase that may be encoded by the heterologous sequences of the present invention. Illustrative examples of suitable nucleotide sequences that may be used as heterologous sequences include but are not limited to: (AY693650 from Oscimum basilicum) and (AY906866, REGION: 10…1887 from Pseudotsuga menziesii). In some embodiments, the product is abietadiene, amorphadiene, carene, α-farnesene, β- farnesene, farnesol, geraniol, geranylgeraniol, isoprene, linalool, limonene, myrcene, nerolidol, ocimene, patchoulol, β-pinene, sabinene, γ-terpinene, terpinolene, menthol, eucalyptol, citronellol, citronellal, or valencene. In some embodiments, the product is β-farnesene. In some embodiments, the product is myrcene. In some embodiments, the product is pinene. In some embodiments, the product is limonene. Methods of Production Provided herein are methods for producing one or more compounds in a culture medium, where the compound may be a water-immiscible compound. The methods described herein may include a number of steps to isolate the compound produced by the cells in the culture medium. These steps may include introducing into the bioreactor a water-immiscible solvent, wherein the organic compound partitions into the water-immiscible solvent, forming a mixture of the aqueous culture medium and the water-immiscible solvent, selecting a portion of the mixture, separating a plurality of the host cells from the portion of the mixture selected, returning the plurality of the host cells to the bioreactor, and recovering the organic compound from the portion of the mixture selected. While the processes and systems provided herein have been described with respect to a limited number of embodiments, the specific features of one embodiment should not be attributed to other embodiments of the processes or systems. No single embodiment is representative of all aspects of the methods or systems. In certain embodiments, the processes can include numerous steps not mentioned herein. In some embodiments, the processes do not include any steps not described herein. Variations and modifications from the described embodiments exist. The product may be produced by culturing cells capable of synthesizing the product in a bioreactor, such as fermentation vessel. The bioreactor may have a capacity of between 1,000,000 L and 0.25 L; for example, the bioreactor may have a capacity of between 0.25 L and 500,000 L, 0.25 L and 100,000 L, or 0.25 L and 1,000 L. In some embodiments, the bioreactor has a capacity of 0.25 L. A carbon source may be introduced into the vessel for culturing the cells. In some embodiments, the carbon source is a carbohydrate. In other embodiments, the carbon source is an Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT alcohol (e.g., ethanol, glycerol, etc.). In other embodiments, the carbon source is obtained from second generation sugars (e.g., digestions of lignocellulose). In some embodiments, the carbon source is continuously introduced into the vessel. The carbon source may be introduced into the vessel by way of a pump. The carbon source may be introduced into the vessel at a rate of from about 0.01 g total reducing sugar (TRS) / L / hour to about 25 g TRS / L / hour. In some embodiments, the carbon source may be introduced into the vessel at a rate of from about 0.05 g TRS / L / hour to about 20 g TRS / L / hour. In some embodiments, the carbon source may be introduced into the vessel at a rate of less than 0.15 g TRS / L / hour, such as a rate of from about 0.01 g TRS / L / hour to about 0.15 g TRS / L / hour. The carbon source that is being introduced into the vessel may have a concentration of about 3% (w / v) to about 80% (w / v) of total reducing sugar; for example, it may have a concentration of about 30% (w / v) of total reducing sugar, or it may have a concentration of about 60% (w / v) of total reducing sugar. In some embodiments, culturing conditions are anaerobic. In other embodiments, culturing conditions are aerobic or microaerobic and the culture medium includes cells which consume oxygen. They may consume oxygen at a rate of from about 25 mmol / L / hr to about 300 mmol / L / hr (e.g., about 25 mmol / L / hr to about 225 mmol / L / hr, about 25 mmol / L / hr to about 200 mmol / L / hr, about 25 mmol / L / hr to about 175 mmol / L / hr, about 25 mmol / L / hr to about 150 mmol / L / hr, about 25 mmol / L / hr to about 125 mmol / L / hr, about 25 mmol / L / hr to about 100 mmol / L / hr, about 25 mmol / L / hr to about 75 mmol / L / hr, about 75 mmol / L / hr to about 250 mmol / L / hr, about 100 mmol / L / hr to about 250 mmol / L / hr, about 125 mmol / L / hr to about 250 mmol / L / hr, about 150 mmol / L / hr to about 250 mmol / L / hr, about 175 mmol / L / hr to about 250 mmol / L / hr, about 200 mmol / L / hr to about 250 mmol / L / hr, or about 225 mmol / L / hr to about 250 mmol / L / hr). In some embodiments, the host cells in the fermentation composition consume oxygen at a rate of from about 90 mmol / L / hr to about 130 mmol / L / hr (e.g., about 90 mmol / L / hr to about 120 mmol / L / hr, about 90 mmol / L / hr to about 110 mmol / L / hr, about 90 mmol / L / hr to about 100 mmol / L / hr, about 100 mmol / L / hr to about 130 mmol / L / hr, about 110 mmol / L / hr to about 130 mmol / L / hr, or about 120 mmol / L / hr to about 130 mmol / L / hr). For example, the cells in the culture medium consume oxygen at a rate of from about 90 mmol / L / hr to about 130 mmol / L / hr. In some embodiments, the cells in the culture medium consume oxygen at a rate of from about 110 mmol / L / hr. Aqueous Phase Separation The aqueous phase containing the cells may be separated from the oil-emulsion phase containing the product using gravity separation. The gravity separation process may include cell sedimentation. In some embodiments, the gravity separation is achieved using a gravity separation device. The gravity settling device may include an inlet tube that is in fluid communication with, and that receives the portion of the mixture from, the bioreactor; a settling chamber that is in fluid communication with, and that receives the portion of the mixture from, the inlet tube; an outlet at the bottom of the settling chamber that is in fluid communication with the vessel; and an outlet at the top of the settling chamber that is in fluid communication with an effluent vessel. The gravity settling Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT device may also include an overflow outlet at the top of the inlet tube that is in fluid communication with the effluent vessel, whereby upon introduction into the inlet tube of an excess of the mixture that exceeds the volume of the settling chamber, the excess mixture flows through the overflow outlet and into the effluent vessel. The settling chamber and the inlet tube may be joined at an angle of from about 60oto about 120o(e.g., 60oto 110o, 60oto 90o, 60oto 80o, 60oto 70o, 70oto 120o, 80oto 120o, 90oto 120o, 100oto 120o, or 80oto 110o), optionally wherein the settling chamber and the inlet tube are joined at an angle of 90o. Furthermore, the settling chamber comprises one or more baffles; for example, the settling chamber may include between 1 and 10 baffles (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10), or the baffle may comprise one or more sloped surfaces. The settling chamber may have one or more sloped sides. In some embodiments, the settling chamber is gradually sloped between the outlet at the top of the settling chamber that is in fluid communication with an effluent vessel and the inlet tube. The slope between the outlet at the top of the settling chamber that is in fluid communication with an effluent vessel and the inlet tube may be constant, or the slope may be variable. In some embodiments, the settling chamber is gradually sloped between the outlet at the bottom of the settling chamber that is in fluid communication with the bioreactor and the inlet tube. The slope between the outlet at the bottom of the settling chamber that is in fluid communication with the bioreactor and the inlet tube may be constant, or the slope may be variable. The settling chamber may include a cone comprising the outlet at the top of the settling chamber that is in fluid communication with the effluent vessel and an inverted cone comprising the outlet at the bottom of the settling chamber that is in fluid communication with the bioreactor. There may also be a cylinder between the cone and the inverted cone. The inlet tube may intersect with the settling chamber at the interface of the cone and the inverted cone. In some embodiments, the inlet tube intersects with the settling chamber at the cylinder between the cone and the inverted cone. The inlet tube and the outer edge of the cone may form an angle of greater than 0° and less than, or equal to, 90°. For example, the inlet tube and the outer edge of the cone form an angle of from about 25° to about 75° (e.g., 25° to 65°, 25° to 55°, 25° to 45°, 25° to 35°, 35° to 75°, 45° to 75°, 55° to 75°, 65° to 75°, 35° to 65°, 45° to 55°, or 30° to 60°). In some embodiments, the inlet tube and the outer edge of the cone form an angle of from about 35° to about 55° (e.g., 35° to 50°, 35° to 45°, 35° to 40°, 40° to 55°, 45° to 55°, 50° to 55°, or 40° to 50°). In some embodiments, the inlet tube and the outer edge of the cone form an angle of about 45°. In some embodiments, the cone has an angle of greater than 0° and less than 90° relative to an axis between the outlet at the bottom of the settling chamber that is in fluid communication with the bioreactor and the outlet at the top of the settling chamber that is in fluid communication with an effluent vessel. The cone may have an angle of greater than 5° and less than 65° (e.g., 5° to 10°, 5° to 15°, 5° to 20°, 5° to 25°, 5° to 50°, 25° to 65°, 25° to 55°, 25° to 45°, 25° to 35°, 35° to 75°, 45° to 75°, 55° to 75°, 65° to 75°, 35° to 65°, 45° to 55°, or 30° to 60°) relative to an axis between the outlet at the bottom of the settling chamber that is in fluid communication with the bioreactor and the outlet at the top of the settling chamber that is in fluid communication with an effluent vessel. For example, the cone may have an angle of greater than 5° and less than 45° (e.g., 5° to 40°, 5° to 35°, 5° to 30°, 5° to 25°, 5° to 20°, 5° to 15°, 5° to 10°, 10° to Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT 45°, 15° to 45°, 20° to 45°, 25° to 45°, 30° to 45°, 35° to 45°, 40° to 45°, 10° to 30°, or 15° to 40°) relative to an axis between the outlet at the bottom of the settling chamber that is in fluid communication with the bioreactor and the outlet at the top of the settling chamber that is in fluid communication with an effluent vessel. The inlet tube and the outer edge of the inverted cone may form an angle of greater than 0° and less than, or equal to, -90°. In some embodiments, the inlet tube and the outer edge of the inverted cone form an angle of from about -25° to about -75° (e.g., -25° to -65°, -25° to -55°, -25° to - 45°, -25° to -35°, -35° to -75°, -45° to -75°, -55° to -75°, -65° to -75°, -35° to -55°, or -40 to -60°). In some embodiments, the inlet tube and the outer edge of the inverted cone form an angle of from about -35° to about -55° (e.g., -35° to -50°, -35° to -45°, -35° to -40°, -40° to -55°, -45° to -55°, or -40° to -45°). In some embodiments, the inlet tube and the outer edge of the inverted cone form an angle of about -45°. The inverted cone may have an angle of greater than 0° and less than 90° relative to an axis between the outlet at the bottom of the settling chamber that is in fluid communication with the bioreactor and the outlet at the top of the settling chamber that is in fluid communication with an effluent vessel. For example, the inverted cone may have an angle of greater than 5° and less than 65° (e.g., 25° to 65°, 25° to 55°, 25° to 45°, 25° to 35°, 35° to 75°, 45° to 75°, 55° to 75°, 65° to 75°, 35° to 65°, 45° to 55°, or 30° to 60°) relative to an axis between the outlet at the bottom of the settling chamber that is in fluid communication with the bioreactor and the outlet at the top of the settling chamber that is in fluid communication with an effluent vessel. The inverted cone may have an angle of greater than 5° and less than 45° (e.g., 5° to 40°, 5° to 35°, 5° to 30°, 5° to 25°, 5° to 20°, 5° to 15°, 5° to 10°, 10° to 45°, 15° to 45°, 20° to 45°, 25° to 45°, 30° to 45°, 35° to 45°, 40° to 45°, 10° to 30°, or 15° to 40°) relative to an axis between the outlet at the bottom of the settling chamber that is in fluid communication with the bioreactor and the outlet at the top of the settling chamber that is in fluid communication with an effluent vessel. The inlet tube may be connected to the settling chamber by way of a cone. The cone may have an angle of greater than 0° and less than 90° relative to an axis between inlet tube and the settling chamber. In some embodiments, the cone has an angle of greater than 5° and less than 65° (e.g., 25° to 65°, 25° to 55°, 25° to 45°, 25° to 35°, 35° to 75°, 45° to 75°, 55° to 75°, 65° to 75°, 35° to 65°, 45° to 55°, or 30° to 60°) relative to an axis between inlet tube and the settling chamber. For example, the cone may have an angle of greater than 5° and less than 45° (e.g., 5° to 40°, 5° to 35°, 5° to 30°, 5° to 25°, 5° to 20°, 5° to 15°, 5° to 10°, 10° to 45°, 15° to 45°, 20° to 45°, 25° to 45°, 30° to 45°, 35° to 45°, 40° to 45°, 10° to 30°, or 15° to 40°) relative to an axis between inlet tube and the settling chamber. The cone connecting the inlet tube to the settling chamber may be perpendicular to the settling chamber. In some embodiments, the cells may be sedimented at a rate of about 0.03 mm / min or greater. For example, the cells are sedimented at a rate of from about 0.003 mm / min or greater, optionally wherein the cells are sedimented at a rate of from about 0.003 mm / min to about 0.5 mm / min (e.g., about 0.003 mm / min to about 0.4 mm / min, about 0.003 mm / min to about 0.3 mm / min, about 0.003 mm / min to about 0.2 mm / min, about 0.003 mm / min to about 0.1 mm / min, about 0.003 mm / min to about 0.05 mm / min, about 0.003 mm / min to about 0.01 mm / min, about 0.003 mm / min to about 0.005 mm / min, about 0.005 mm / min to about 0.5 mm / min, about 0.01 mm / min to Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT about 0.5 mm / min, about 0.05 mm / min to about 0.5 mm / min, about 0.1 mm / min to about 0.5 mm / min about 0.2 mm / min to about 0.5 mm / min, about 0.3 mm / min to about 0.5 mm / min, or about 0.4 mm / min to about 0.5 mm / min). A pump may be used in the settling device. In some embodiments, the portion of the mixture including the culture medium is delivered to the inlet tube by way of a pump. In some embodiments, the portion of the mixture including the culture medium is delivered to the inlet tube without a pump. In some embodiments, the portion of the mixture including the culture medium is delivered to the inlet tube by making use of a pressure differential. In some embodiments, the water-immiscible solvent is removed from the settling chamber and delivered through the outlet at the top of the settling chamber to the effluent bottle by way of a pump. The settling chamber may be able hold between 0.1 L and 50 L (e.g., 0.1 L and 40 L, 0.1 L and 30 L, 0.1 L and 20 L, 0.1 L and 10 L, 0.1 L and 1 L, 1 L and 50 L, 10 L and 50 L, 20 L and 50 L, 30 L and 50 L, 40 L and 50 L, 20 L and 40 L, 10 L and 30 L, 30 L and 40 L, 10 L and 40 L, 20 L to 40 L, 1 L to 10 L, 1 L to 30 L, 1 L to 20 L, or 5 L to 40 L). For example, thesettling chamber may hold from 1.5 L to 3 L (e.g., 1.5±0.5 L, 2.0±0.5 L, 2.5±0.5 L, or 3.0±0.5 L). In some embodiments, the settling chamber is greater than 20 L. In some embodiments, the settling chamber is from 20 L to 50 L (e.g., 20 L to 45 L, 20 L to 40 L, 20 L to 35 L, 20 L to 30 L, 20 L to 25 L, 25 L to 50 L, 30 L to 50 L, 35 L to 50 L, 40 L to 50 L, 45 L to 50 L, 30 L to 40 L, 25 L to 35 L, or 35 L to 45 L). Pinch valves may be used, for example, to limit the entry of air bubbles into the separation area of the separation device and to control the amount of the mixture including the culture medium entering and exiting the separation device. These pinch valves may be controlled by timers. In some embodiments, the opening and closing of pinch valves may be automated by monitoring the volume of liquid in the bubble trap. The volume of liquid in the bubble trap may be monitored, for example, using a float switch, a light curtain sensor, or sensors for monitoring capacitance. The culture medium may be oxygenated. Oxygenating of the culture medium may be achieved by pumping air into the bioreactor. The air may be compressed air. The compressed air may be delivered by pressure. The bioreactor may be kept at a pressure of from about 5 psi to about 25 psi (e.g., 5 psi to 20 psi, 5 psi to 15 psi, 5 psi to 10 psi, 10 psi to 25 psi, 15 psi to 25 psi, 20 psi to 25 psi, 10 psi to 20 psi, or 15 psi to 25 psi). For example, the pressure may be between 5 psi and 10 psi (e.g., 5 psi to 9 psi, 5 psi to 8 psi, 5 psi to 7 psi, 5 psi to 6 psi, 6 psi to 10 psi, 7 psi to 10 psi, 8 psi to 10 psi, 9 psi to 10 psi, 6 psi to 8 psi, or 6 psi to 9 psi). In some embodiments, the pressure of the bioreactor is maintained at a pressure of between 10 psi to 20 psi (e.g., 10 psi to 18 psi, 10 psi to 16 psi, 10 psi to 14 psi, 10 psi to 12 psi, 12 psi to 20 psi, 14 psi to 20 psi, 16 psi to 20 psi, 18 psi to 20 psi, 12 psi to 16 psi, or 14 psi to 18 psi). In some embodiments, the bioreactor may be kept at a pressure of from about 0.1 psi to about 5 psi (e.g., 0.1 psi to 1 psi, 0.1 psi to 2 psi, 0.1 psi to 3 psi, 0.1 psi to 4 psi, 0.1 psi to 5 psi, 1 psi to 5 psi, 2 psi to 5 psi, 3 psi to 5 psi, 4 psi to 5 psi, 1 psi to 3 psi, or 1 psi to 4 psi). The culture medium may be mixed using an impeller. Furthermore, the culture medium and the water-immiscible solvent may be mixed using an impeller. In some embodiments, the culture medium and the water-immiscible solvent are mixed using a bubble column, wherein the bubble Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT column is a gas distributor. The bubble column may be located in a vessel with the water-immiscible solvent and culture medium and may sparge gas into the water-immiscible solvent and / or culture medium. Producing the product in a culture medium may include contacting the culture medium with a water-immiscible solvent. In some instances, the product is a water-immiscible compound. The water-immiscible solvent may be added to the culture medium to a final concentration of water- immiscible solvent of from about 0.5% (v / v) to about 50% (v / v) e.g., about 0.5% (v / v) to about 10% (v / v), about 0.5% (v / v) to about 20% (v / v), about 0.5% (v / v) to about 30% (v / v), about 0.5% to about 40% (v / v), about 40% (v / v) to about 50% (v / v), about 30% (v / v) to about 50% (v / v), about 20% (v / v) to about 50% (v / v), or about 10% (v / v) to about 50% (v / v)). In some embodiments, the water-immiscible solvent is added to the culture medium to a final concentration of water-immiscible solvent of from about 5% (v / v) to about 25% (v / v). The water-immiscible solvent may have a log(Kd) value of from about 1 to about 15, where Kdis the partition coefficient for the product between the water-immiscible solvent and the culture medium. For example, the log (Kd) may be about 1.5, about 1.6, about 1.7, about 1.8, about 1.9, about 2, about 2.1, about 2.2, about 2.3, about 2.4, about 2.5, about 2.6, about 2.7, about 2.8, about 2.9, or about 3. In some embodiments, the water-immiscible solvent may log(Kd) value of from about 2 to about 3. For example, the water-immiscible solvent has a log(Kd) value of about 2, about 2.1, about 2.2, about 2.3, about 2.4, about 2.5, about 2.6, about 2.7, about 2.8, about 2.9, or about 3. In some embodiments, the water-immiscible solvent may log(Kd) value of from about 3 to about 4. For example, the water-immiscible solvent has a log(Kd) value of about 3, about 3.1, about 3.2, about 3.3, about 3.4, about 3.5, about 3.6, about 3.7, about 3.8, about 3.9, or about 4. In some embodiments, the water-immiscible solvent may log(Kd) value of from about 4 to about 5. For example, the water- immiscible solvent has a log(Kd) value of about 4, about 4.1, about 4.2, about 4.3, about 4.4, about 4.5, about 4.6, about 4.7, about 4.8, about 4.9, or about 5. In some embodiments, the water- immiscible solvent may log(Kd) value of from about 5 to about 6. For example, the water-immiscible solvent has a log(Kd) value of about 5, about 5.1, about 5.2, about 5.3, about 5.4, about 5.5, about 5.6, about 5.7, about 5.8, about 5.9, or about 6. In some embodiments, the water-immiscible solvent may log(Kd) value of from about 6 to about 6. For example, the water-immiscible solvent has a log(Kd) value of about 6, about 6.1, about 6.2, about 6.3, about 6.4, about 6.5, about 6.6, about 6.7, about 6.8, about 6.9, or about 7. In some embodiments, the water-immiscible solvent may log(Kd) value of from about 7 to about 8. For example, the water-immiscible solvent has a log(Kd) value of about 7, about 7.1, about 7.2, about 7.3, about 7.4, about 7.5, about 7.6, about 7.7, about 7.8, about 7.9, or about 8. In some embodiments, the water-immiscible solvent may log(Kd) value of from about 8 to about 9. For example, the water-immiscible solvent has a log(Kd) value of about 8, about 8.1, about 8.2, about 8.3, about 8.4, about 8.5, about 8.6, about 8.7, about 8.8, about 8.9, or about 9. In some embodiments, the water-immiscible solvent may log(Kd) value of from about 9 to about 10. For example, the water-immiscible solvent has a log(Kd) value of about 9, about 9.1, about 9.2, about 9.3, about 9.4, about 9.5, about 9.6, about 9.7, about 9.8, about 9.9, or about 10. In some embodiments, the water-immiscible solvent may log(Kd) value of from about 10 to about 11. For example, the water- Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT immiscible solvent has a log(Kd) value of about 10, about 10.1, about 10.2, about 10.3, about 10.4, about 10.5, about 10.6, about 10.7, about 10.8, about 10.9, or about 11. In some embodiments, the water-immiscible solvent may log(Kd) value of from about 11 to about 12. For example, the water- immiscible solvent has a log(Kd) value of about 11, about 11.1, about 11.2, about 11.3, about 11.4, about 11.5, about 11.6, about 11.7, about 11.8, about 11.9, or about 12. In some embodiments, the water-immiscible solvent may log(Kd) value of from about 12 to about 13. For example, the water- immiscible solvent has a log(Kd) value of about 12, about 12.1, about 12.2, about 12.3, about 12.4, about 12.5, about 12.6, about 12.7, about 12.8, about 12.9, or about 13. In some embodiments, the water-immiscible solvent may log(Kd) value of from about 13 to about 14. For example, the water- immiscible solvent has a log(Kd) value of about 13, about 13.1, about 13.2, about 13.3, about 13.4, about 13.5, about 13.6, about 13.7, about 13.8, about 13.9, or about 14. In some embodiments, the water-immiscible solvent may log(Kd) value of from about 14 to about 15. For example, the water- immiscible solvent has a log(Kd) value of about 14, about 14.1, about 14.2, about 14.3, about 14.4, about 14.5, about 14.6, about 14.7, about 14.8, about 14.9, or about 15. The product may have a log(D) value of from about 1 to about 15 (e.g., about 1.1, 1.2, 1.3, 1.4, 1.5, 1.6, 1.7, 1.8, 1.9, 2, 2.1, 2.2, 2.3, 2.4, 2.5, 2.6, 2.72.8, 2.9, 3, 3.1, 3.2, 3.3, 3.4, 3.5, 3.6, 3.7, 3.8, 3.9, 4, 4.1, 4.2, 4.3, 4.4, 4.5, 4.6, 4.7, 4.8, 4.9, 5, 5.1, 5.2, 5.3, 5.4, 5.5, 5.6, 5.7, 5.8, 5.9, 6, 6.1, 6.2, 6.3, 6.4, 6.5, 6.6, 6.7, 6.8, 6.9, 7, 7.1, 7.2, 7.3, 7.4, 7.5, 7.6, 7.7, 7.8, 7.9, 8, 8.1, 8.2, 8.3, 8.4, 8.5, 8.6, 8.7, 8.8, 8.9, 9, 9.1, 9.2, 9.3, 9.4, 9.5, 9.6, 9.7, 9.8, 9.9, 10, 10.1, 10.2, 10.3, 10.4, 10.5, 10.6, 10.7, 10.8, 10.9, 11, 11.1, 11.2, 11.3, 11.4, 11.5, 11.6, 11.7, 11.8, 11.9, 12, 12.1, 12.2, 12.3, 12.4, 12.5, 12.6, 12.7, 12.8, 12.9, 13, 13.1, 13.2, 13.3, 13.4, 13.5, 13.6, 13.7, 13.8, 13.9, 14, 14.1, 14.2, 14.3, 14.4, 14.5, 14.6, 14.7, 14.8, 14.9, or 15. The water-immiscible solvent may be an alcohol. For example, the water-immiscible solvent may be a C10-C20 alcohol (e.g., C10 alcohol, C11 alcohol, C12 alcohol, C13 alcohol, C14 alcohol, C15 alcohol, C16 alcohol, C17 alcohol, C18 alcohol, C19 alcohol, or C20 alcohol). In some embodiments, the water-immiscible solvent may be a C12-C18 alcohol (e.g., C12 alcohol, C13 alcohol, C14 alcohol, C15 alcohol, C16 alcohol, C17 alcohol, or C18 alcohol). In some embodiments, the water-immiscible solvent is DRAKEOL 10. In some embodiments, the water-immiscible solvent is ESTEREX A32. In some embodiments, the water-immiscible solvent is DURASYN 164. In other embodiments, the water- immiscible solvent is a vegetable oil. In some embodiments, the water-immiscible solvent is corn oil, sunflower oil, soybean oil, mineral oil, polyalphaolefin, dodecane, hexadecane, oleyl alcohol, butyl oleate, dibutyl phthalate, dodecanol, dioctyl phthalate, farnesene, or isopropyl myristate. In some embodiments, the organic product may be isolated from the culture medium using a filter, optionally wherein the filter is located in the bioreactor. In some embodiments, the filter separates the water-immiscible solvent from the culture medium in the fermentation vessel. In some embodiments, the filter is capable of separating at least a portion of the product from at least a portion of the cells in the bioreactor. Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT Enzymes of Exemplary Biosynthetic Pathways The host cells described herein may express one or more enzymes of a biosynthetic pathway capable of producing a product of interest, including by fermentation. In some embodiments, for example, host cells of the disclosure (e.g., yeast cells) may naturally express some of the enzymes of the biosynthetic pathway for a given isoprenoid. Such host cells may be modified to express the remaining or heterologous enzymes of the biosynthetic pathway. In some embodiments, for instance, a host cell (e.g., a yeast cell) may naturally express many of the enzymes of the biosynthetic pathway of a desired isoprenoid (e.g., a terpene), and the host cells may be modified so as to express the remaining enzymes of the biosynthetic pathway for the desired isoprenoid by providing the cells with one or more heterologous nucleic acid molecules that, together, encode the remaining enzymes of the biosynthetic pathway. The one or more enzymes may be from the mevalonate-dependent (MEV) pathway or the 1-deoxy-D-xylulose 5-diphosphate (DXP) pathway. The host cells described herein may be modified to express one or more enzymes of the MEV biosynthetic pathway. Host 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 host 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 host 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 host 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; Saccharomyces cerevisiae), and (NC_001145: complement (115734.118898; Saccharomyces cerevisiae). In some embodiments, the host cells include a heterologous nucleotide sequence encoding an enzyme that can convert mevalonate into mevalonate 5-phosphate, e.g., a mevalonate kinase. Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT 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 host 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 host 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 host cells include one or more heterologous nucleotide sequences encoding more than one enzyme of the MEV pathway. In some embodiments, the host cell includes one or more heterologous nucleotide sequences encoding two enzymes of the MEV pathway. In some embodiments, the host 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 host cell includes one or more heterologous nucleotide sequences encoding three enzymes of the MEV pathway. In some embodiments, the host cell includes one or more heterologous nucleotide sequences encoding four enzymes of the MEV pathway. In some embodiments, the host cell includes one or more heterologous nucleotide sequences encoding five enzymes of the MEV pathway. In some embodiments, the host cell includes one or more heterologous nucleotide sequences encoding six enzymes of the MEV pathway. In some embodiments, the host 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 host cells described herein may be modified to express one or more enzymes of the DXP biosynthetic pathway. Host 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 host cell which is not modified with one or enzymes of the DXP biosynthetic pathway. In some embodiments, the host 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). In some embodiments, the host cell includes a heterologous nucleotide sequence encoding an enzyme, e.g., l-deoxy-D-xylulose-5-phosphate synthase, which can condense pyruvate with D- Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT 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 host 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 host 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 host 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 host 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 host 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)-buteny 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 host cell includes a heterologous nucleotide sequence encoding an enzyme, e.g., isopentyl / dimethylallyl diphosphate synthase, which can convert l-hydroxy-2-methyl- 2-(E)-butenyl-4-diphosphate into either IPP or its isomer, DMAPP. Illustrative examples of nucleotide Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT sequences include but are not limited to: (AY062212; Escherichia coli) and (NC_002947, locus tag PP0606; Pseudomonas putida KT2440). In some embodiments, the host cell includes one or more heterologous nucleotide sequences encoding more than one enzyme of the DXP pathway. In some embodiments, the host cell includes one or more heterologous nucleotide sequences encoding two enzymes of the DXP pathway. In some embodiments, the host cell includes one or more heterologous nucleotide sequences encoding three enzymes of the DXP pathway. In some embodiments, the host cell includes one or more heterologous nucleotide sequences encoding four enzymes of the DXP pathway. In some embodiments, the host cell includes one or more heterologous nucleotide sequences encoding five enzymes of the DXP pathway. In some embodiments, the host cell includes one or more heterologous nucleotide sequences encoding six enzymes of the DXP pathway. In some embodiments, the host cell includes one or more heterologous nucleotide sequences encoding five enzymes of the DXP pathway. In some embodiments, the host cell includes one or more heterologous nucleotide sequences encoding seven enzymes of the DXP pathway. In some embodiments, "cross talk" (or interference) between the host 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 host cell relies exclusively on the DXP pathway for synthesizing IPP, and a MEV pathway is introduced to provide additional IPP. Such a host 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 host cell produces IPP via the MEV pathway, either exclusively or in combination with the DXP pathway. In other embodiments, a host cell’s DXP pathway is functionally disabled so that the host 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 host 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 host 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; Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT ATCC 14579), (AJ243739; Citrus sinensis), (AY534745; Clarkia breweri), (AY953508; fps pini), (DQ286930; Lycopersicon esculentum), (AF182828; Mentha x piperita), (AF182827; Mentha x piperita), (MPI249453; Mentha x piperita), (PZE431697, Locus CAD24425; Paracoccus 862; Vi tis vinifera), and (AF203881, Locus In some embodiments, the host 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 host 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), Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT (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), (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 host 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- Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT 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-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 α-pinene synthase. Illustrative examples of suitable nucleotide sequences include but are not limited to: (+) apinene synthase (AF543530, REGION: 1.1887; Pinus taeda), (-)α-pinene synthase (AF543527, REGION: 32.1921; Pinus taeda), and (+) / (-)α-pinene synthase (AGU87909, REGION: 6111892;Abies grandis). In some embodiments, the heterologous nucleotide encodes a β-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). Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT 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. 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 host cell. In some embodiments, one or more heterologous nucleic acids encoding one or more enzymes are present within one or more plasmids. In some embodiments, for example, host cells of the disclosure (e.g., yeast cells) may naturally express some of the enzymes of the biosynthetic pathway for a given cannabinoid. Such host cells may be modified to express the remaining or heterologous enzymes of the biosynthetic pathway. In some embodiments, for instance, a host cell (e.g., a yeast cell) may naturally express many of the enzymes of the biosynthetic pathway of a desired cannabinoid, and the host cells may be modified so as to express the remaining enzymes of the biosynthetic pathway for the desired cannabinoid 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 host cell includes 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 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 host 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 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 host cell includes an AAE, TKS, OAC, CBGaS, and a GPP synthase. The cannabinoid pathway is described in Keasling et al. (WO 2018 / 200888). Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT 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 a product, such as an isoprenoid or terpene, 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 bioreactor may be used including a stirred tank bioreactor, an airlift bioreactor, a bubble fermentor, or any combination thereof. In particular embodiments utilizing 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 microbial cell culture 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 culture 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 overlay or other water-immiscible solvent. In other embodiments, the suitable medium is supplemented with antifoam. In some embodiments, the suitable medium is supplemented with 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). In some embodiments, the carbon source is a monosaccharide (simple sugar), a disaccharide, a polysaccharide, a non-fermentable carbon source, or one or more combinations thereof. Non-limiting examples of suitable monosaccharides include glucose, galactose, mannose, fructose, ribose, and combinations thereof. Non-limiting examples of suitable disaccharides include sucrose, lactose, maltose, trehalose, cellobiose, and combinations thereof. Non-limiting examples of suitable polysaccharides include starch, glycogen, cellulose, chitin, and combinations thereof. Non- limiting examples of suitable non-fermentable carbon sources include acetate, ethanol, and glycerol. Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT The concentration of a carbon source, such as glucose or sucrose, in the culture medium should promote cell growth, but not be so high as to repress growth of the microorganism used. Typically, cultures are run with a carbon source, such as glucose or sucrose, being added at levels to achieve the desired level of growth and biomass. Production of compounds, such as isoprenoids, may also occur in these culture conditions, but at undetectable levels (with detection limits being about <0.1 g / l). In other embodiments, the concentration of a carbon source, such as glucose or sucrose, in the culture medium is greater than about 1 g / L, preferably greater than about 2 g / L, and more preferably greater than about 5 g / L. In addition, the concentration of a carbon source, such as glucose or sucrose, in the culture medium is typically less than about 100 g / L, preferably less than about 50 g / L, and more preferably less than about 20 g / L. It should be noted that references to culture component concentrations can refer to both initial and / or ongoing component concentrations. In some cases, it may be desirable to allow the culture medium to become depleted of a carbon source during culture. Sources of assimilable nitrogen that can be used in a suitable culture medium include, but are not limited to, simple nitrogen sources, organic nitrogen sources and complex nitrogen sources. Such nitrogen sources include anhydrous ammonia, ammonium hydroxide, ammonium salts and substances of animal, vegetable and / or microbial origin. Suitable nitrogen sources include, but are not limited to, protein hydrolysates, microbial biomass hydrolysates, peptone, yeast extract, ammonium sulfate, urea, and amino acids. Typically, the concentration of the nitrogen sources in the culture medium is greater than about 0.1 g / L, preferably greater than about 0.25 g / L, and more preferably greater than about 1.0 g / L. Beyond certain concentrations, however, the addition of a nitrogen source to the culture medium is not advantageous for the growth of the microorganisms. As a result, the concentration of the nitrogen sources, in the culture medium is less than about 20 g / L, preferably less than about 10 g / L and more preferably less than about 5 g / L. Further, in some instances it may be desirable to allow the culture medium to become depleted of the nitrogen sources during culture. The effective culture medium can contain other compounds such as inorganic salts, vitamins, trace metals, or growth promoters. Such other compounds can also be present in carbon, nitrogen, or mineral sources in the effective medium or can be added specifically to the medium. The culture medium can also contain a suitable phosphate source. Such phosphate sources include both inorganic and organic phosphate sources. Preferred phosphate sources include, but are not limited to, phosphate salts such as mono or dibasic sodium and potassium phosphates, ammonium phosphate, and mixtures thereof. Typically, the concentration of phosphate in the culture medium is greater than about 1.0 g / L, preferably greater than about 2.0 g / L, and more preferably greater than about 5.0 g / L. Beyond certain concentrations, however, the addition of phosphate to the culture medium is not advantageous for the growth of the microorganisms. Accordingly, the concentration of phosphate in the culture medium is typically less than about 20 g / L, preferably less than about 15 g / L, and more preferably less than about 10 g / L. A suitable culture medium can also include a source of magnesium, preferably in the form of a physiologically acceptable salt, such as magnesium sulfate heptahydrate, although other Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT magnesium sources in concentrations that contribute similar amounts of magnesium can be used. Typically, the concentration of magnesium in the culture medium is greater than about 0.5 g / L, preferably greater than about 1.0 g / L, and more preferably greater than about 2.0 g / L. Beyond certain concentrations, however, the addition of magnesium to the culture medium is not advantageous for the growth of the microorganisms. Accordingly, the concentration of magnesium in the culture medium is typically less than about 10 g / L, preferably less than about 5 g / L, and more preferably less than about 3 g / L. Further, in some instances, it may be desirable to allow the culture medium to become depleted of a magnesium source during culture. In some embodiments, the culture medium can also include a biologically acceptable chelating agent, such as the dihydrate of trisodium citrate. In such an instance, the concentration of a chelating agent in the culture medium is greater than about 0.2 g / L, preferably greater than about 0.5 g / L, and more preferably greater than about 1 g / L. Beyond certain concentrations, however, the addition of a chelating agent to the culture medium is not advantageous for the growth of the microorganisms. Accordingly, the concentration of a chelating agent in the culture medium is typically less than about 10 g / L, preferably less than about 5 g / L, and more preferably less than about 2 g / L. The culture medium can also initially include a biologically acceptable acid or base to maintain the desired pH of the culture medium. Biologically acceptable acids include, but are not limited to, hydrochloric acid, sulfuric acid, nitric acid, phosphoric acid, and mixtures thereof. Biologically acceptable bases include, but are not limited to, ammonium hydroxide, sodium hydroxide, potassium hydroxide, and mixtures thereof. In some embodiments, the base used is ammonium hydroxide. The culture medium can also include a biologically acceptable calcium source, including, but not limited to, calcium chloride. Typically, the concentration of the calcium source, such as calcium chloride, dihydrate, in the culture medium is within the range of from about 5 mg / L to about 2000 mg / L, preferably within the range of from about 20 mg / L to about 1000 mg / L, and more preferably in the range of from about 50 mg / L to about 500 mg / L. The culture medium can also include sodium chloride. Typically, the concentration of sodium chloride in the culture medium is within the range of from about 0.1 g / L to about 5 g / L, preferably within the range of from about 1 g / L to about 4 g / L, and more preferably in the range of from about 2 g / L to about 4 g / L. In some embodiments, the culture medium can also include trace metals. Such trace metals can be added to the culture medium as a stock solution that, for convenience, can be prepared separately from the rest of the culture medium. Typically, the amount of such a trace metals solution added to the culture medium is greater than about 1 mL / L, preferably greater than about 5 mL / L, and more preferably greater than about 10 mL / L. Beyond certain concentrations, however, the addition of trace metals to the culture medium is not advantageous for the growth of the microorganisms. Accordingly, the amount of such a trace metals solution added to the culture medium is typically less than about 100 mL / L, preferably less than about 50 mL / L, and more preferably less than about 30 mL / L. It should be noted that, in addition to adding trace metals in a stock solution, the individual Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT components can be added separately, each within ranges corresponding independently to the amounts of the components dictated by the above ranges of the trace metals solution. The culture medium can include other vitamins, such as pantothenate, biotin, calcium pantothenate, inositol, para-aminobenzoic acid, nicotinic acid, pyridoxine-HCl, and thiamine-HCl. Such vitamins can be added to the culture medium as a stock solution that, for convenience, can be prepared separately from the rest of the culture medium. Beyond certain concentrations, however, the addition of vitamins to the culture medium is not advantageous for the growth of the microorganisms. The culture medium may include trace metals, such as iron, copper, cobalt, zinc, selenium, chromium, iodine, and molybdenum. Such trace metals can be added to the culture medium as a stock solution that, for convenience, can be prepared separately from the rest of the culture medium. In some embodiments, the culture medium may include an antifoam or surfactant. In some embodiments, the surfactant may be an anionic surfactant; for example, the surfactant may be alkyl- naphthalene sulfonate, alkyl benzene sulfonate, or the like. In some embodiments, the surfactant is a nonionic surfactant. Suitable surfactants include biocompatible nonionic surfactants such as Brij (e.g., polyoxyethylene (4) lauryl ether, also known as Brij-30; polyoxyethylene (2) oleyl ether; polyoxyethylene (2) stearyl ether; etc.); micelles; and the like. In some embodiments, the surfactant is a secondary ether polyol. In some embodiments, the surfactant is TERGITOL L-62 (Dow Chemical Company). In some embodiments, the surfactant is TERGITOL L-81 (Dow Chemical Company). In some embodiments, the surfactant is a JarcolTMalcohol. In some embodiments, the surfactant is TERGAZYME (Alconox), which may be used in an amount of between 0% (w / v) and about 1% (w / v). The methods described herein can be performed in conventional culture modes, which include, but are not limited to, batch, fed-batch, cell recycle, continuous and semi-continuous. In some embodiments, the cell culture is carried out in fed-batch mode. In such a case, some of the components of the medium are depleted during culture, including pantothenate during the production stage of the fermentation. In some embodiments, the culture may be supplemented with relatively high concentrations of such components at the outset, for example, of the production stage, so that growth and / or production is supported for a period of time before additions are required. The preferred ranges of these components are maintained throughout the culture by making additions as levels are depleted by culture. Levels of components in the culture medium can be monitored by, for example, sampling the culture medium periodically and assaying for concentrations. Alternatively, once a standard culture procedure is developed, additions can be made at timed intervals corresponding to known levels at particular times throughout the culture. As will be recognized by those in the art, the rate of consumption of nutrient increases during culture as the cell density of the medium increases. Moreover, to avoid introduction of foreign microorganisms into the culture medium, addition is performed using aseptic addition methods, as are known in the art. In addition, anti-foaming agent may be added during the culture. The temperature of the culture medium can be any temperature suitable for growth of the genetically modified cells and / or production of compounds of interest. For example, prior to inoculation of the culture medium with an inoculum, the culture medium can be brought to and Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT maintained at a temperature in the range of from about 20oC to about 45oC (e.g., 20oC, 21oC, 22oC, 23oC, 24oC, 25oC, 26oC, 27oC, 28oC, 29oC, 30oC, 31oC, 32oC, 33oC, 34oC, 35oC, 36oC, 37oC, 38oC, 39oC, and 40oC). In some embodiments, the temperature is preferably in the range of from about 25oC to about 40oC (e.g., 25oC, 26oC, 27oC, 28oC, 29oC, 30oC, 31oC, 32oC, 33oC, 34oC, 35oC, 36oC, 37oC, 38oC, 39oC, and 40oC) and more preferably in the range of from about 28oC to about 32oC (e.g., 28oC, 29oC, 30oC, 31oC, and 32oC). In some embodiments, the temperature is preferably in the range of 25oC to 40oC (e.g., 25oC, 26oC, 27oC, 28oC, 29oC, 30oC, 31oC, 32oC, 33oC, 34oC, 35oC, 36oC, 37oC, 38oC, 39oC, and 40oC) and more preferably in the range from about 35oC to 39oC (e.g., 35oC, 36oC, 37oC, 38oC, and 39oC). The pH of the culture medium can be controlled by the addition of acid or base to the culture medium. In such cases when ammonia is used to control pH, it also conveniently serves as a nitrogen source in the culture medium. Preferably, the pH is maintained from about 3.0 to about 9.0 (e.g., 3.0±1.0, 4.0±1.0, 5.0±1.0, 6.0±1.0, 7.0±1.0, 8.0±1.0, and 9.0±1.0), more preferably from about 3.5 to about 7.0 (e.g., 3.5±0.5, 4.0±0.5, 4.5±0.5, 5.0±0.5, 5.5±0.5, 6.0±0.5, 6.5 ±0.5, and 7.0±0.5,) and most preferably from about 4.0 to about 6.5. In some embodiments, the carbon source concentration, such as the glucose concentration, of the culture medium is monitored during culture. Glucose or sucrose concentration of the culture medium can be monitored using known techniques, such as, for example, use of the glucose oxidase enzyme test or high-pressure liquid chromatography, which can be used to monitor glucose concentration in the supernatant, e.g., a cell-free component of the culture medium. As stated previously, the carbon source concentration should be kept below the level at which cell growth inhibition occurs. Although such concentration may vary from organism to organism, for glucose as a carbon source, cell growth inhibition occurs at glucose concentrations greater than at about 60 g / L and can be determined readily by trial. Accordingly, when glucose is used as a carbon source the glucose is preferably fed to the fermenter and maintained below detection limits. Alternatively, the glucose concentration in the culture medium is maintained in the range of from about 1 g / L to about 100 g / L, more preferably in the range of from about 2 g / L to about 50 g / L, and yet more preferably in the range of from about 5 g / L to about 20 g / L. Although the carbon source concentration can be maintained within desired levels by addition of, for example, a substantially pure glucose solution, it is acceptable, and may be preferred, to maintain the carbon source concentration of the culture medium by addition of aliquots of the original culture medium. The use of aliquots of the original culture medium may be desirable because the concentrations of other nutrients in the medium (e.g., the nitrogen and phosphate sources) can be maintained simultaneously. Likewise, the trace metals concentrations can be maintained in the culture medium by addition of aliquots of the trace metals solution. Host Cell Strains Any suitable host cell may be used in the practice of the present invention. Illustrative examples of suitable host 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, Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT 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. 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. 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, Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT 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, 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 Example 1. Fermentation Conditions In the lab, the fermentation process started with a sequence of inoculum expansions, starting with thawed seed vial cultures, and over time expanding the cell mass through shake flask stages before the main production fermentor inoculation. At the pilot-plant scale this inoculum expansion could utilize initial fermentor and / or seed fermentor stages depending on the mass of final inoculum needed for production inoculation. In general, the perfusion separation device was connected to the Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT production fermenter as a peripheral device, where the aqueous medium and cells were constantly being recycled back into the fermenter while the light phase (overlay-emulsion containing product) was being removed. Lab Scale (0.5 L) Fermentation Setup As shown in FIG.1, the set up consisted of a main production fermenter (MF) connected to a glass tube separation in-situ product removal (ISPR) device. The fermenter air out condenser was connected to a glass off-gas trap where the off-gas bubbles flowed from the bottom. The top of the off-gas trap was connected to a mass spectrometer. The glass separation device was positioned at an angle, as shown in FIG.1. There were 2 pumps employed in this process. An external pump was used for pumping out from the fermenter into the separation device. The second pump was connected to the top of the separation device and used for pumping out effluent to an effluent bottle. Two pinch valves were installed as depicted in FIG.1. These were controlled by an external on / off controller. These valves were controlled by a timer, where the return valve would close, and the purge valve would open for a short amount of time to allow bubble purging by filling up the short arm of the glass tube separation device. An alternative configuration of the separation device is shown in FIG.2. This configuration does not require pinch valves. However, bubbles may accumulate at the top, which may require a faster effluent rate to operate. This would not affect the separation efficiency at lab scale. In addition to feedstock and base addition, overlay feed was connected to the fermenter for continuous addition through the digital control unit (DCU) pump. As overlay was pumped out from the top of the separation device, static charge could build up around the tube. To mitigate this, grounding wires were attached to the metal prong of the effluent bottle, as well as to the prongs of overlay inlet bottle. An off-gas trap was used to collect the myrcene evaporated and made it from the fermenter through the condenser. The off-gas trap was kept at room temperature. Lab Scale (0.5 L, 2 L) Fermentor Operation The fermentation was run as an ISPR process in continuous mode. Inside the separation device, the main force acting to separate the oil, emulsion, and aqueous layers was gravity. The hydrophobicity and density differences between the oil, emulsion, and aqueous layers also drove their separation. With a long enough retention time in a low turbulence state, the difference in specific gravities naturally caused the oil and liquid to separate into distinct layers. Whole cell broth mixture (containing the aqueous liquid, oil, and emulsion) was pumped from the fermenter into the separation device, where the aqueous liquid and oils and emulsion separated by gravity inside the separation device’s setting zone. Most of the aqueous broth and biomass returned to the tank, and most of the oils (added water-immiscible solvent and product) were removed out of the top of the separation device. Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT The residence time of liquids in the separation area of the separation device as well as the rate of oils supply and removal from the separation area are important for the separation device performance. Thus, care must be taken to control both the whole cell broth recirculation rate and the oils and emulsion effluent rate. For the system to be balanced, the rate at which whole cell broth is introduced into the separation area must approximate the sum of the rate at which effluent is pumped into the effluent bottle and the rate at which the aqueous medium and cells are returned to the main fermentor. Further, to enable separation and product removal, the effluent flow rate needs to be slower than the rate of oils separation from aqueous layer. Fermenter Parameters • Feeding strategy: constant feed to keep pace with consumption. • Temperature: 30°C. • Air flow rate: 0.5-0.67 VVM (L / L / min). • Agitation: controlled to achieve a measured OUR of 110 mmol O2 / L / hr. • pH: 5.0 with the addition of NH4OH. • Antifoam: TERGITOL L-81. • Overlay: DRAKEOL 10 or DURASYN 164. • Run time: 7 days. Once inoculated, the ISPR pumps were not started for the first day while the culture biomass built up. No sampling was needed around this time since the effluent bottle was empty. Overlay addition was then initiated based on one of three approaches: standard, ISPR V1, and ISPR V2 (see Example 2). The pump on the effluent stream was controlled by tank weight. When the tank weight was below the setpoint, the pump stopped turning; this ensured that the fermenter weight was always kept constant (except when sampled). Lastly, the short arm of the glass separation device was monitored. If it filled up too fast or didn’t fill up, the valve timer was adjusted as appropriate. Example 2. Results – Daily Bolus (“ISPR V1”) and Continuous Overlay Perfusion (“ISPR V2”) Both Improve Yield and Productivity Over a Single Initial Dose of Overlay Standard fermentation was a fed- batch process with a single initial dose of overlay in the fermenter. ISPR Version 1 (ISPR V1) was standard fermentation with a separation device, and a single bolus of overlay introduced into the fermenter daily with continuous removal of effluent at a fixed rate. ISPR Version 2 (ISPR V2) was a standard fermentation with a separation device, and continuous overlay perfusion and continuous removal of effluent at a fixed rate. In all processes, upon drawing and sampling from the fermentor, fresh overlay was added to replace the draw volumes. In a representative standard, non-ISPR fermentation for myrcene production, the fermentation cell culture experienced myrcene inhibition around day 3, and the culture metabolism was severely reduced after day 4, presumably due to myrcene accumulation in the tank (FIG.3). Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT Utilizing the ISPR V1 (daily bolus) approach to product removal improved the fermentation performance: the oxygen uptake rate (OUR) was improved (FIG.4A), and a ~50% improvement in yield and ~100% improvement in productivity (FIG.5A and FIG.5B) were observed. Compared to the standard process, product titers in the fermentation tank (exclusive of effluent bottle) decreased over time in the ISPR V1 process as it was removed from the fermentation tank into the effluent bottle (FIG.4B). The process was improved further using the ISPR V2 approach (continuous overlay perfusion). In the first continuous addition experiment, overlay was added at a rate of approximately 0.5 L overlay / L broth / day instead of as a bolus. The fermentation OUR remained high throughout the fermentation (FIG.6), an indication that the culture was much healthier. As a result, fermentation key performance indicators (KPIs) with ISPR V2 approach improved another 28% in yield and 115% in productivity (FIG.7A and FIG.7B) compared to ISPR V1, and a total of 84% increase in yield and 320% increase in productivity over the standard process. In both ISPR V1 and ISPR V2, culture performance was improved from the combination of reduced myrcene titers in the fermentor, reducing exposure of the cells to the product. In addition, continuous removal of the overlay reduced the cells’ exposure more. In ISPR V1, most of the fresh overlay added at the beginning of each day was removed in about 10 hours. As the overlay concentration decreased in the tank, it became harder to separate the top layer from aqueous broth. Since it was more difficult to remove the myrcene, the cells were exposed to the myrcene for a longer duration, thereby impacting cell health and metabolism. In ISPR V2, fresh overlay was constantly being introduced, and myrcene was constantly removed as it was being produced. Example 3. Relationship Between Overlay Perfusion Rate and Yield and Productivity In Example 2, the overlay perfusion rate of 0.5 L / L / day was used to establish the ISPR V2 process. Since increased or decreased perfusion rate might impact the fermentation performance, a range of overlay perfusion rates were tested to establish the relationship between overlay perfusion rate and fermentation KPIs (yield and productivity) to explore the myrcene strain’s production limit. The correlation could potentially then be used to understand the production cost implications. Perfusion rates from 0.06 to 0.8 L / L / day were tested. The KPIs vs. overlay perfusion rate curve shows that fermentation KPIs increases to a plateau as overlay perfusion rate increased (FIG.8A and FIG.8B). This was expected because at high rates of removal, product inhibition was minimized; at low rates, the performance was similar to standard fermentations without ISPR. It was interesting further that once the perfusion rate exceeded 0.8 L / L / day, improvements in fermentation performance began to level off. It is reasonable to assume that at these high perfusion rates, the fermentation began to reach the limit of the strain’s capability – essentially, the broth was fully detoxified. Example 4. Vertical Delta Separator (VDS) Design The main force acting to separate the oil, emulsion, and aqueous layers is gravity. The hydrophobicity and density differences between the oil, emulsion, and aqueous layers also drive their Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT separation. With a long enough retention time in a low turbulence state, the difference in specific gravities will naturally cause the oil and liquid to separate into distinct layers. The original glass tube design shown in FIG.1 was designed to maximize biomass settling and return to the main fermentor. With regards to phase separation, within the tested overlay perfusion rates shown in FIG.8A and FIG.8B, the original glass tube design worked well in separating the overlay-emulsion layer from the broth. However, the overlay-broth mixture had a residence time of 300 minutes. Visually, the overlay emulsion layer separated out from the broth within minutes, so it was hypothesized that a separation device with a smaller internal volume could also separate the mixture efficiently. As a proof of concept, a vertical delta separator (VDS) model was fabricated (FIG.9) with an internal volume of about 1 / 4 of the original separation device (FIG.1) and a residence time of 75 minutes. The VDS separation device was shorter, and wider in the middle to allow for better gravity separation than the narrower width glass tube. Thus, the VDS design possessed the advantage of less stringent design and operating conditions compared to the original glass tube design. It will be understood by those of skill in the art that additional features (ports, venting routes, baffles, etc.) could be incorporated into the VDS or glass tube designs. From previous experiments, the effluent contained about 90% overlay, and then became steady around 70% as the fermentation proceeded. Effluent from runs with the reverse separation device (control) and VDS were similar and agreed with previous results (FIG.10). As the VDS internal volume was about 1 / 4 of the reverse separation device, this indicated that the glass tube separation device was oversized for aqueous-overlay separation. The rate of separation was much faster than the residence time through the separation device under nonturbulent flow. Moreover, the fermentation performance between the two were comparable as expected (FIG.11A and FIG.11B). A further advantage of the VDS design was the simplification of the separation process due to the fact that the need for pinch valves and systems to control the pinch valves were eliminated. Example 5. Scale up of Myrcene Fermentation with ISPR at Pilot Scale Similar to the lab scale, at pilot scale, the fermentation process started with a sequence of inoculum expansions, starting with thawed seed vial cultures, and over time expanding the cell mass through shake flask stages before the main production fermentor inoculation. At the pilot-plant scale this inoculum expansion could utilize initial fermentor and / or seed fermentor stages depending on the mass of final inoculum needed for production inoculation. In general, the perfusion separation device was connected to the production fermenter as a peripheral device, where the aqueous medium and cells were constantly being recycled back into the fermenter while the light phase (overlay-emulsion containing product) was being removed. 20 L Fermentation Setup As shown in FIG.12, the set up consisted of a main production fermenter (MF) connected to an off-gas trap (Off-gas Trap 1) as well as two pumps. The feed pump (Pump 1) pumped cell broth from the main production fermenter to the separation device (Settling Unit) connected aseptically to Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT the 20 L fermenter. The return pump (Pump 2) pumped cells and aqueous material back into the main production fermenter. The flow rate difference between the two pumps resulted in the separation device overflowing settled material (Effluent) into a collection tank (Effluent Collection Vessel). Another off-gas trap could be connected to the collection tank to capture any volatile product vapors, minimizing the vapor release into the open air. In addition to feedstock and base addition through the digital control unit (DCU) pump, the overlay feed was connected to the fermenter for continuous addition through an external pump. 20 L Fermentation Operation The fermentation was run as an ISPR process in continuous mode. As with the lab scale fermentation operation, inside the separation device (1.5 L commercial settler), the main force acting to separate the oil, emulsion, aqueous, and cell layers was gravity. The immiscibility and density differences between the layers was needed to allow gravity to separate the layers. Additionally, cones within the settling device significantly increase the settling area and act as baffles to reduce the turbulence from pumping cell broth into the device, both of which significantly improve the separation of the layers. Cell broth (containing the oil, emulsion, aqueous, and cells) was pumped from the fermentor into the separation device, where the layers are separated by gravity. Most of the aqueous broth and cells were pumped back into the fermenter while most of the oils (added water-immiscible solvent and product) overflowed out of the top of the separation device and collected as effluent in the effluent collection vessel. The residence time of the liquids in the separation device as well as the flow rate of the material being fed, recycled, and overflowed from the device were controlled by peristaltic pumps. After inoculation, the culture was allowed to build biomass for one day before the separation device feed and return pumps were started. Keeping the ISPR process off until one day into the fermentation process was intentional, as it reduced the amount of overlay needed to run the fermentation without negatively impacting the fermentation KPIs (yield and productivity), as the amount of toxic product in the fermenter by day one was far below the point at which the culture was impacted. 300 L Fermentation Setup As shown in FIG.13A, the set up consisted of a main production fermenter (MF) connected to an off-gas trap (Off-Gas Trap 1), a valve (Valve 1), and a pump (Pump 1). Cell broth flowed from the main production fermenter through valve 1 to the separation device (Settling Unit), either commercially available settling devices (2.1 L or 24 L) or a 2.4 L VDS (FIG.13B), by pressure, as the fermenter was pressurized. The pressure of the main production fermenter at 300 L scale had feedback control to maintain a steady pressure, reducing deviations in settling unit feed flow rate. The valve between fermenter and settling unit was used to turn off flow of the broth during the fermentation growth phase or if a leak was observed. The return pump (Pump 1) pumped cells and aqueous material back into the main production fermenter. The flow rate difference between the feed to the settling unit and return of the settling unit to the main fermenter resulted in the separation Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT device overflowing settled material (Effluent) into a collection tank (Effluent Collection Vessel). A valve (valve 2) was implemented between the settling unit and the effluent collection tank. This valve was regulated by the weight of the main fermenter tank (monitored by the SCADA unit), where it would open when the tank exceeded a specific weight setpoint and would close when the tank weight was below that setpoint, effectively setting the average effluent flow rate to the combined rate of feedstock and overlay addition to the fermenter. 300 L Fermenter Operation The fermentation was run as an ISPR process in continuous mode. As with the lab and 20 L scale fermentation operations, inside the separation device, the main force acting to separate the oil, emulsion, aqueous, and cell layers was gravity. The immiscibility and density differences between the layers was needed to allow gravity to separate the layers. Additionally, cones within the commercially available settling devices (2 L to 24 L) significantly increase the settling area and act as baffles to reduce the turbulence from high flow rate of cell broth into the device, both of which significantly improve the separation of the layers. The pilot scale VDS settler mainly rely on gravity settling of the layers. Cell broth (containing the oil, emulsion, aqueous, and cells) flowed from the fermentor through the valve into the separation device, where the layers were separated by gravity. Most of the aqueous broth and cells were pumped back into the fermenter while most of the oils (added water- immiscible solvent and product) overflowed out of the top of the separation device and collected as effluent in the effluent collection vessel. Fermenter Parameters (20-300 L scale): • Feeding strategy: constant feed to keep pace with consumption. • Temperature: 30°C • Air flow rate: 0.5 VVM (L / L / min) • Agitation: controlled to achieve a measured OUR of 110 mmol O2 / L / hr • pH: 5.0 with the addition of NH4OH • Antifoam: TERGITOL L-81 • Overlay: DRAKEOL 10 • Overlay perfusion rate: 0.3 L / L / day • Main Fermenter back pressure: 7.5 – 15 psi • Run time: 5 to 7 days Materials and Methods Pilot Scale Settlers: Commercially available cell settlers: The device was either single use disposable or reusable stainless steel with variable volume capacity and contained inverted cones to improve its settling capabilities. VDS: Device was composed of commercially available stainless steel sanitary fittings and reducers. Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT SCADA definition: Supervisory Control and Data Acquisition. These systems were comprised of computers, instrumentation, and graphical interfaces to enable monitoring and controlling process commands. Results Relationship Between Settling Device Separation Performance and Fermentation KPIs The separation performance of a settling device had significant impacts on the fermentation KPIs (yield and productivity). Two separation performance indicators used to evaluate a settling device were the effluent overlay fraction and cell broth overlay fraction. While the effluent overlay fraction was largely dependent on the fraction of overlay added over the fermentation, it could be used to determine when the separation performance reached equilibrium. At equilibrium, the cell broth overlay fraction was the most impactful indicator of separator unit performance. Lower cell broth overlay fractions at equilibrium reflect better separation performance, as the separator unit achieved the equilibrium effluent overlay fraction with less overlay in the cell broth. Lower cell broth overlay fractions were also preferrable for the fermentation process, as it resulted in a lower amount of toxic product in the cell broth, reduced the inhibitory effects to the culture. For 20 L ISPR fermentations with a commercial disposable settler unit, as shown in FIG.14B, the effluent produced by the settler was composed largely of overlay, matching the separation performance observed at lab scale. In FIG.14A, the whole cell broth (WCB) overlay fraction decreases over time, indicating the overlay was being separated out more quickly than it was replenished, demonstrating the settling device was not the limiting factor in the fermentation with ISPR. This successful scale up was further confirmed on the fermentation side as the product yield (%) on sugar and productivities (g / L / h) observed matched those that were observed at lab scale (FIG. 15A and FIG.15B). For 300 L ISPR fermentations were carried out with reusable stainless steel commercial settlers (2 L to 24 L) and a VDS as separation devices. The separation performance at 300 L scale using commercial settlers matched that of the 20 L fermentations and 2 L lab scale fermentations (FIG.16A and FIG.16B). The fermentation performance KPIs, product yield (%) on sugar and productivities (g / L / h), between the 2 L, 20 L and 300 L scales also matched closely (FIGS.15A, 15B, 17A, and 17B). To reduce the footprint of the settling unit at scale, smaller commercially available and in- house assembled VDS separation devices were tested at 300 L scale. The separation performance between the two commercially available settling devices and VDS were similar, though the separation of the pilot scale VDS unit was slightly less effective (FIGS.18 and 19). The fermentation performance with the pilot scale VDS was slightly lower, 84% product yield and 77% productivity relative to lab scale and the commercial settler units (FIGS.20A and 20B) tested at 300 L scale. This was due to the less clear separation of the immiscible solvent and relatively high accumulation of product into the fermenter cell broth. However, the smaller settling units, commercial ones and VDS, are promising, as there is room to optimize the operations and implement process control improvements to enhance the separation and fermentation performance. Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT Example 6. Linalool Fermentation with Lab Scale ISPR It was demonstrated at the 2 L scale that the performance of linalool fermentation can be significantly improved by the ISPR technology over the batch overlay process, given that linalool is a toxic monoterpene molecule that has broad applications including fragrances, flavorings, and pest control. The linalool fermentation and isolation were performed using continuous overlay perfusion (ISPR V2) as described above in Example 2. The fermentation was run in 2L fermenters as an ISPR process in continuous mode. Inside the separation device, the main force acting to separate the oil, emulsion, aqueous, and cell layers was gravity. The immiscibility and density differences between the layers was needed to allow gravity to separate the layers. Cell broth (containing the oil, emulsion, aqueous, and cells) was pumped from the fermentor into the separation device, where the layers are separated by gravity. Most of the aqueous broth and cells were pumped back into the fermenter while most of the oils (added water- immiscible solvent and product) overflowed out of the top of the separation device and collected as effluent in the effluent collection vessel. The residence time of the liquids in the separation device as well as the flow rate of the material being fed, recycled, and overflowed from the device were controlled by peristaltic pumps. After inoculation, the culture was allowed to build biomass for one day before the separation device feed and return pumps were started or device feed and return pumps were started at a very low rate. Keeping the ISPR process off (or at a very low rate) until one day into the fermentation process was intentional, as it reduced the amount of overlay needed to run the fermentation without negatively impacting the fermentation KPIs (yield and productivity), as the amount of toxic product in the fermenter by day one was far below the point at which the culture was impacted. The water-immiscible solvent of ESTEREX A32 or DRAKEOL 10 was added to the fermenter in a bolus at the start of the fermentation (control, non ISPR process). Improved results were noted in the performance of the ISPR V2 process for linalool fermentation when DRAKEOL 10 was used (FIGS.22 A to D). For both ESTEREX A32 and DRAKEOL 10, the product yield (%), volumetric productivity (g / L / hr), and total product produced (g) was measured for when a batch process was used and when ISPR was used (FIGS.21A-21C and FIGS.22A-22C) and the total improvement achieved by using ISPR is summarized in FIGS.21D and 22D. Linalool Fermenter Parameters (2 L scale): • Feeding strategy: constant feed to keep pace with consumption. • Temperature: 30°C • Air flow rate: 0.5 VVM (L / L / min) • Agitation: controlled to achieve a measured OUR up to 90 mmol O2 / L / hr • pH: 5.0 with the addition of NH4OH • Antifoam: TERGITOL L-81 • Overlay: DRAKEOL 10 or ESTEREX A32 Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT • Overlay perfusion rate: 0.5 L / L / day • Run time: 7 days

Claims

Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT CLAIMS 1. A method of producing an organic compound comprising: (a) culturing a population of host cells in an aqueous culture medium in a bioreactor, wherein the host cells produce the organic compound, (b) introducing into the bioreactor a water-immiscible solvent, wherein the organic compound partitions into the water-immiscible solvent, (c) forming a mixture of the aqueous culture medium and the water-immiscible solvent, (d) selecting a portion of the mixture, (e) separating a plurality of the host cells from the portion of the mixture selected in (d), (f) returning the plurality of the host cells to the bioreactor, and (g) recovering the organic compound from the portion of the mixture selected in (d).

2. The method of claim 1, wherein introducing the water-immiscible solvent occurs once during the culturing of the host cells.

3. The method of claim 1, wherein introducing the water-immiscible solvent occurs multiple times during the culturing of the host cells.

4. The method of claim 3, wherein introducing the water-immiscible solvent occurs during the culturing of the host cells at a frequency selected from once daily, twice daily, three times daily, four times daily, five times daily, six times daily, seven times daily, eight times daily, nine times daily, ten times daily, eleven times daily, and twelve times daily.

5. The method of claim 1, wherein introducing the water-immiscible solvent occurs continuously during culturing of the host cells.

6. The method of claim 5, wherein introducing the water-immiscible solvent occurs continuously at a rate of between 0.01 to 1.5 liters per liter of mixture per day.

7. The method of claim 6, wherein introducing the water-immiscible solvent occurs continuously at a rate of between 0.03 to 1.3 liters per liter of mixture per day.

8. The method of claim 7, wherein introducing the water-immiscible solvent occurs continuously at a rate of between 0.05 to 1.0 liters per liter of mixture per day.

9. The method of claim 8, wherein introducing the water-immiscible solvent occurs continuously at a rate of between 0.06 to 0.9 liters per liter of mixture per day.

10. The method of any one of claims 1-9, wherein the organic compound is susceptible to chemical modification in the aqueous culture medium.Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT 11. The method of any one of claims 1-10, wherein the organic compound is inhibitory to the host cells.

12. The method of any one of claims 1-11, wherein the organic compound is a terpene.

13. The method of claim 12, wherein the terpene is a C5-C40 terpene.

14. The method of claim 13, wherein the terpene is a C5-C20 terpene.

15. The method of claim 14, wherein the terpene is a C10-C15 terpene.

16. The method of claim 12, wherein the terpene is a hemiterpene, monoterpene, sesquiterpene, diterpene, sesterterpene, triterpene, tetraterpene, or polyterpene.

17. The method of claim 16, wherein the terpene is a monoterpene.

18. The method of any one of claims 1-11, wherein the organic compound is an isoprenoid.

19. The method of claim 18, wherein the isoprenoid is a C5-C20 isoprenoid.

20. The method of claim 19, wherein the isoprenoid is a C10-C15 isoprenoid.

21. The method of claim 18, wherein the isoprenoid is a hemiterpenoid, monoterpenoid, sesquiterpenoid, diterpenoid, sesterterpenoid, triterpenoid, tetraterpenoid, or polyterpenoid.

22. The method of claim 21, wherein the isoprenoid is a monoterpenoid.

23. The method of any one of claims 1-11, wherein the organic compound is abietadiene, anethole, amorphadiene, carene, carvacrol, creosol, cuminaldehyde, eugenol, α-farnesene, β- farnesene, farnesol, geranial, geraniol, geranylgeraniol, hinokitiol, isoprene, isoprenol, linalool, limonene, myrcene, nerolidol, ocimene, patchoulol, perillyl alcohol, α-pinene, β-pinene, sabinene, γ- terpinene, terpinolene, thujone, menthol, neral, nerol, eucalyptol, citronellol, citronellal, carvone, isopulegol, valencene, or a salvinorin.

24. The method of claim 23, wherein the organic compound is β-farnesene.

25. The method of claim 23, wherein the organic compound is myrcene.

26. The method of claim 23, wherein the organic compound is pinene.Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT 27. The method of claim 23, wherein the organic compound is limonene.

28. The method of claim 23, wherein the organic compound is menthol.

29. The method of claim 23, wherein the organic compound is citronellal.

30. The method of claim 23, wherein the organic compound is citronellol.

31. The method of claim 23, wherein the organic compound is farnesol.

32. The method of claim 23, wherein the organic compound is terpinene.

33. The method of claim 23, wherein the organic compound is terpinolene.

34. The method of claim 23, wherein the organic compound is geraniol.

35. The method of claim 23, wherein the organic compound is linalool.

36. The method of any one of claims 1-35, wherein the host cells are selected from the group consisting of a bacterial cell, a fungal cell, an algal cell, an insect cell, and a plant cell.

37. The method of claim 36, wherein the host cells are yeast cells.

38. The method of claim 37, wherein the yeast cells are Saccharomyces cerevisiae.

39. The method of claim any one of claims 1-38, the method further comprising repeating steps (a) through (g) a plurality of times, optionally wherein the method comprises repeating steps (a) through (g) continuously or discontinuously.

40. The method of any one of claims 1-38, the method further comprising repeating steps (b) through (g) a plurality of times, optionally wherein the method comprises repeating steps (b) through (g) continuously or discontinuously.

41. The method of any one of claims 1-38, the method further comprising repeating steps (b) through (e) a plurality of times, optionally wherein the method comprises repeating steps (b) through (e) continuously or discontinuously.

42. The method of any one of claims 1-41, wherein the separating a plurality of the host cells from the portion of the mixture selected in (d) occurs by way of a gravity separation process.Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT 43. The method of claim 42, wherein the gravity separation process comprises cell sedimentation.

44. The method of claim 43, wherein the cell sedimentation is achieved using a gravity settling device.

45. The method of claim 44, wherein the gravity settling device comprises: (i) an inlet tube that is in fluid communication with, and that receives the portion of the mixture from, the bioreactor; (ii) a settling chamber that is in fluid communication with, and that receives the portion of the mixture from, the inlet tube; (iii) an outlet at the bottom of the settling chamber that is in fluid communication with the bioreactor; and (iv) an outlet at the top of the settling chamber that is in fluid communication with an effluent vessel.

46. The method of claim 45, wherein the gravity settling device further comprises an overflow outlet at the top of the inlet tube that is in fluid communication with the effluent vessel, whereby upon introduction into the inlet tube of an excess of the mixture that exceeds the volume of the settling chamber, the excess mixture flows through the overflow outlet and into the effluent vessel.

47. The method of claim 45 or 46, wherein the settling chamber and the inlet tube are joined at an angle of from about 60oto about 120o, optionally wherein the settling chamber and the inlet tube are joined at an angle of 90o.

48. The method of any one of claims 45-47, wherein the settling chamber comprises one or more baffles.

49. The method of any one of claims 45-48, wherein the settling chamber is gradually sloped between the outlet at the top of the settling chamber that is in fluid communication with an effluent vessel and the inlet tube.

50. The method of any one of claims 45-49, wherein the slope between the outlet at the top of the settling chamber that is in fluid communication with an effluent vessel and the inlet tube is constant.

51. The method of any one of claims 45-49, wherein the slope between the outlet at the top of the settling chamber that is in fluid communication with an effluent vessel and the inlet tube is variable.Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT 52. The method of any one of claims 45-51, wherein the settling chamber is gradually sloped between the outlet at the bottom of the settling chamber that is in fluid communication with the bioreactor and the inlet tube.

53. The method of any one of claims 45-52, wherein the slope between the outlet at the bottom of the settling chamber that is in fluid communication with the bioreactor and the inlet tube is constant.

54. The method of any one of claims 45-53, wherein the slope between the outlet at the bottom of the settling chamber that is in fluid communication with the bioreactor and the inlet tube is variable.

55. The method of any one of claims 45-54, wherein the cell sedimentation comprises: (i) introducing the portion of the mixture into the inlet tube; (ii) allowing the plurality of the host cells to flow to the bottom of the settling chamber and, subsequently, to return to the bioreactor through the outlet at the bottom of the settling chamber; and (iii) removing the water-immiscible solvent from the settling chamber through the outlet at the top of the settling chamber and delivering the water-immiscible solvent to the effluent bottle.

56. The method of any one of claims 45-55, wherein the portion of the mixture is delivered to the inlet tube by way of a pump.

57. The method of any one of claims 45-56, wherein the water-immiscible solvent is removed from the settling chamber and delivered through the outlet at the top of the settling chamber to the effluent bottle by way of a pump.

58. The method of any one of claims 45-57, wherein the settling chamber is between 0.1 L and 50 L.

59. The method of claim 58, wherein the settling chamber is from 1.5 L to 3 L.

60. The method of any one of claims 45-57, wherein the settling chamber is greater than 20 L.

61. The method of claim 60, wherein the settling chamber is from 20 L to 50 L.Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT 62. The method of any one of claims 1-61, wherein the bioreactor is between 0.1 L and 1000 L.

63. The method of any one of claims 1-62, wherein the bioreactor is greater than 200 L.

64. The method of any one of claims 1-63, wherein the method results in performance enhancement of the host cells relative to a reference method which does not comprise steps (b) through (g).

65. The method of claim 64, wherein the method results in a performance enhancement of the host cells of from about 0.5% to about 500% relative to a reference method which does not comprise steps (b) through (g).

66. The method of any one of claims 1-65, wherein the method results in an increase in yield of the organic compound relative to a reference method which does not comprise steps (b) through (g).

67. The method of claim 66, wherein the method results in an increase in yield of the organic compound from about 0.5% to about 500% relative to a reference method which does not comprise steps (b) through (g).

68. The method of any one of claims 1-67, wherein the method results in an increase in productivity of the organic compound relative to a reference method which does not comprise steps (b) through (g).

69. The method of claim 68, wherein the method results in an increase in productivity of the organic compound from about 0.5% to about 500% relative to a reference method which does not comprise steps (b) through (g).

70. The method of any one of claims 1-69, wherein the host cells in the aqueous culture medium in the bioreactor consume oxygen at a rate of from about 25 mmol / L / hr to about 250 mmol / L / hr.

71. The method of claim 70, wherein the host cells in the aqueous culture medium in the bioreactor consume oxygen at a rate of from about 90 mmol / L / hr to about 130 mmol / L / hr.

72. The method of claim 71, wherein the host cells in the aqueous culture medium in the bioreactor consume oxygen at a rate of from about 110 mmol / L / hr.Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT 73. The method of any one of claims 1-72, wherein the water-immiscible solvent is added to the bioreactor at a rate of from about 0.05 L / L / day to about 1 L / L / day.

74. The method of claim 73, wherein the water-immiscible solvent is added to the bioreactor at a rate of from about 0.2 L / L / day to about 0.6 L / L / day.

75. An organic compound produced using the method of any one of claims 1-74.

76. The compound of claim 75, wherein the organic compound is a terpene.

77. The compound of claim 76, wherein the terpene is a C5-C40 terpene.

78. The compound of claim 77, wherein the terpene is a C5-C20 terpene.

79. The compound of claim 78, wherein the terpene is a C10-C15 terpene.

80. The compound of claim 76, wherein the terpene is a hemiterpene, monoterpene, sesquiterpene, diterpene, sesterterpene, triterpene, tetraterpene, or polyterpene.

81. The compound of claim 80, wherein the terpene is a monoterpene.

82. The compound of claim 75, wherein the organic compound is an isoprenoid.

83. The compound of claim 82, wherein the isoprenoid is a C5-C20 isoprenoid.

84. The compound of claim 83, wherein the isoprenoid is a C10-C15 isoprenoid.

85. The compound of claim 82, wherein the isoprenoid is a hemiterpenoid, monoterpenoid, sesquiterpenoid, diterpenoid, sesterterpenoid, triterpenoid, tetraterpenoid, or polyterpenoid.

86. The compound of claim 85, wherein the isoprenoid is a monoterpenoid.

87. The compound of claim 75, wherein the organic compound is abietadiene, anethole, amorphadiene, carene, carvacrol, creosol, cuminaldehyde, eugenol, α-farnesene, β-farnesene, farnesol, geranial, geraniol, geranylgeraniol, hinokitiol, isoprene, isoprenol, linalool, limonene, myrcene, nerolidol, ocimene, patchoulol, perillyl alcohol, α-pinene, β-pinene, sabinene, γ-terpinene, terpinolene, thujone, menthol, neral, nerol, eucalyptol, citronellol, citronellal, carvone, isopulegol, valencene, or salvinorin.

88. The compound of claim 87, wherein the organic compound is β-farnesene.Attorney Docket No.: 51494-032WO2 Amyris Reference No.: AM-16700 PCT 89. The compound of claim 87, wherein the organic compound is myrcene.

90. The compound of claim 87, wherein the organic compound is pinene.

91. The compound of claim 87, wherein the organic compound is limonene.

92. The compound of claim 87, wherein the organic compound is menthol.

93. The compound of claim 87, wherein the organic compound is citronellal.

94. The compound of claim 87, wherein the organic compound is citronellol.

95. The compound of claim 87, wherein the organic compound is farnesol.

96. The compound of claim 87, wherein the organic compound is terpinene.

97. The compound of claim 87, wherein the organic compound is terpinolene.

98. The compound of claim 87, wherein the organic compound is geraniol.

99. The compound of claim 87, wherein the organic compound is linalool.

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