Patent classifications
C12P17/04
METHOD FOR THE IN VIVO SYNTHESIS OF 4-HYDROXYMETHYLFURFURAL AND DERIVATIVES THEREOF
The present disclosure provides recombinant microorganisms and methods for the production of 4-HMF, 2,4-furandimethanol, furan-2,4-dicarbaldehyde, 4-(hydroxymethyl)furoic acid, 2-formylfuran-4-carboxylate, 4-formylfuran-2-carboxylate, and/or 2,4-FDCA from a carbon source. The method provides for engineered microorganisms that express endogenous and/or exogenous nucleic acid molecules that catalyze the conversion of a carbon source into 4-HMF, 2,4-furandimethanol, furan-2,4-dicarbaldehyde, 4-(hydroxymethyl)furoic acid, 2-formylfuran-4-carboxylate, 4-formylfuran-2-carboxylate, and/or 2,4-FDCA. The disclosure further provides methods of producing polymers derived from 4-HMF, 2,4-furandimethanol, furan-2,4-dicarbaldehyde, 4-(hydroxymethyl)furoic acid, 2-formylfuran-4-carboxylate, 4-formylfuran-2-carboxylate, and/or 2,4-FDCA.
METHODS AND CELLS FOR MICROBIAL PRODUCTION OF PHYTOCANNABINOIDS AND PHYTOCANNABINOID PRECURSORS
The present disclosure relates generally to methods and cell lines for the production of phytocannabinoids, phytocannabinoid precursors or intermediates, or phytocannabinoid analogue. Methods for transformation of host cells, such as yeast cells, are described. Cells may be transformed, for example, with a polynucleotide encoding a polyketide synthase (PKS) enzyme, a polynucleotide encoding an olivetolic acid cyclase (OAC) enzyme, and/or a polynucleotide encoding a prenyltransferase (PT) enzyme; and optionally a polynucleotide encoding an acyl-CoA synthase (Alk) enzyme; a polynucleotide encoding a fatty acyl CoA activating (CsAAE) enzyme; and/or a polynucleotide encoding a THCa synthase (OXC) enzyme.
METHODS AND CELLS FOR MICROBIAL PRODUCTION OF PHYTOCANNABINOIDS AND PHYTOCANNABINOID PRECURSORS
The present disclosure relates generally to methods and cell lines for the production of phytocannabinoids, phytocannabinoid precursors or intermediates, or phytocannabinoid analogue. Methods for transformation of host cells, such as yeast cells, are described. Cells may be transformed, for example, with a polynucleotide encoding a polyketide synthase (PKS) enzyme, a polynucleotide encoding an olivetolic acid cyclase (OAC) enzyme, and/or a polynucleotide encoding a prenyltransferase (PT) enzyme; and optionally a polynucleotide encoding an acyl-CoA synthase (Alk) enzyme; a polynucleotide encoding a fatty acyl CoA activating (CsAAE) enzyme; and/or a polynucleotide encoding a THCa synthase (OXC) enzyme.
Enzyme-catalyzed synthesis of (1S,5R)-bicyclolactone
An enzyme-catalyzed synthesis of (1S,5R)-bicyclolactone. A first genetically-engineered bacterium containing Baeyer-Villiger monooxygenase gene and a second genetically-engineered bacterium containing glucose dehydrogenase gene are constructed and then suspended with culture medium to prepare a first suspension and a second suspension, respectively. The first and second suspensions are centrifuged to respectively produce a first supernatant containing Baeyer-Villiger monooxygenase and a second supernatant containing glucose dehydrogenase, which are mixed. The mixed supernatant is then mixed with a raceme of a substituted bicyclo[3.2.0]-hept-2-en-6-one, a solvent, a hydrogen donor and a cofactor to perform an asymmetric Baeyer-Villiger oxidation to produce the (1S,5R)-bicyclolactone, where an amino acid sequence of the Baeyer-Villiger monooxygenase is shown in SEQ ID NO:1.
Enzyme-catalyzed synthesis of (1S,5R)-bicyclolactone
An enzyme-catalyzed synthesis of (1S,5R)-bicyclolactone. A first genetically-engineered bacterium containing Baeyer-Villiger monooxygenase gene and a second genetically-engineered bacterium containing glucose dehydrogenase gene are constructed and then suspended with culture medium to prepare a first suspension and a second suspension, respectively. The first and second suspensions are centrifuged to respectively produce a first supernatant containing Baeyer-Villiger monooxygenase and a second supernatant containing glucose dehydrogenase, which are mixed. The mixed supernatant is then mixed with a raceme of a substituted bicyclo[3.2.0]-hept-2-en-6-one, a solvent, a hydrogen donor and a cofactor to perform an asymmetric Baeyer-Villiger oxidation to produce the (1S,5R)-bicyclolactone, where an amino acid sequence of the Baeyer-Villiger monooxygenase is shown in SEQ ID NO:1.
Microorganisms for the production of 1,4- butanediol and related methods
The invention provides non-naturally occurring microbial organisms comprising a 1,4-butanediol (BDO) pathway comprising at least one exogenous nucleic acid encoding a BDO pathway enzyme expressed in a sufficient amount to produce BDO and further optimized for expression of BDO. The invention additionally provides methods of using such microbial organisms to produce BDO.
Microorganisms for the production of 1,4- butanediol and related methods
The invention provides non-naturally occurring microbial organisms comprising a 1,4-butanediol (BDO) pathway comprising at least one exogenous nucleic acid encoding a BDO pathway enzyme expressed in a sufficient amount to produce BDO and further optimized for expression of BDO. The invention additionally provides methods of using such microbial organisms to produce BDO.
Isolated bacterial strain of the genus <i>Burkholderia </i>and pesticidal metabolites therefrom
A species of Burkholderia sp with no known pathogenicity to vertebrates but with pesticidal activity (e.g., plants, insects, fungi, weeds and nematodes) is provided. Also provided are natural products derived from a culture of said species and methods of controlling pests using said natural products.
Isolated bacterial strain of the genus <i>Burkholderia </i>and pesticidal metabolites therefrom
A species of Burkholderia sp with no known pathogenicity to vertebrates but with pesticidal activity (e.g., plants, insects, fungi, weeds and nematodes) is provided. Also provided are natural products derived from a culture of said species and methods of controlling pests using said natural products.
Solid form of (-)-Ambrox formed by a bioconversion of homofarnesol in the presence of a biocatalyst
A solid form of (−)-Ambrox formed by a bioconversion process.