C12P7/42

HIGH YIELD ROUTE FOR THE PRODUCTION OF COMPOUNDS FROM RENEWABLE SOURCES
20220389433 · 2022-12-08 ·

Provided herein are methods, compositions, and non-naturally occurring microbial organism for preparing compounds such as α-butanol, butyric acid, succinic acid, 1,4-butanediol, 1-pentanol, pentanoic acid, glutaric acid, 1,5-pentanediol, 1-hexanol, hexanoic acid, adipic acid, 1,6-hexanediol, 6-hydroxy hexanoic acid, ε-Caprolactone, 6-amino-hexanoic acid, ε-Caprolactam, hexamethylenediamine, linear fatty acids and linear fatty alcohols that are between 7-25 carbons long, linear alkanes and linear α-alkenes that are between 6-24 carbons long, sebacic acid and dodecanedioic acid comprising: a) converting a C.sub.N aldehyde and pyruvate to a C.sub.N+3 β-hydroxyketone intermediate through an aldol addition; and b) converting the C.sub.N+3 β-hydroxyketone intermediate to the compounds through enzymatic steps, or a combination of enzymatic and chemical steps.

Prenyltransferase variants with increased thermostability
11518983 · 2022-12-06 · ·

The present disclosure relates to recombinant prenyltransferase enzymes with increased thermostability and activity and the use of these enzymes in compositions and methods for biosynthesis involving prenylation reactions, including compositions and methods for the preparation of cannabinoids.

Prenyltransferase variants with increased thermostability
11518983 · 2022-12-06 · ·

The present disclosure relates to recombinant prenyltransferase enzymes with increased thermostability and activity and the use of these enzymes in compositions and methods for biosynthesis involving prenylation reactions, including compositions and methods for the preparation of cannabinoids.

APPLICATION OF BRANCHED-CHAIN A-KETOACID DEHYDROGENASE COMPLEX IN PREPARATION OF MALONYL COENZYME A
20220380822 · 2022-12-01 ·

An application of a branched-chain α-ketoacid dehydrogenase complex in preparation of malonyl coenzyme A. A method for preparing malonyl-CoA using a branched-chain α-ketoacid dehydrogenase complex, the method comprising introducing a gene encoding a branched-chain α-ketoacid dehydrogenase complex into a biological cell strain to obtain a recombinant cell strain capable of expressing the gene encoding the branched-chain α-ketoacid dehydrogenase complex; culturing the recombinant cell strain to prepare malonyl-CoA; the branched-chain α-ketoacid dehydrogenase complex is the following M1) or M2): M1) a set of proteins consisting of a bkdF protein, a bkdG protein, a bkdH protein and a lpdA1 protein; M2) a set of proteins consisting of a bkdA protein, a bkdB protein, a bkdC protein and the lpdA1 protein. Experimental results show that by using the branched-chain α-ketoacid dehydrogenase complex, not only malonyl-CoA can be prepared, but also a target product using malonyl-CoA as an intermediate product can further be prepared.

PRODUCTION OF MALONATE SEMIALDEHYDE AND DERIVATIVES BY MICROORGANISMS EXPRESSING ASPARTATE 1-DECARBOXYLASE

The present disclosure provides recombinant microorganisms and methods for producing malonate semialdehyde and/or related products, such as ketones, alcohols, organic acids, esters, alkenes, amino acids, and combinations thereof including 3-hydroxypropionic acid, acrylic acid, propionic acid, 1-propanol, acetone, 2-propanol, butanone, 1-butanol, 2-butanol, methyl propionate, 1,3-propanediol, isoamyl alcohol, 1,3-butanediol, 1,4-butanediol, 2,3-butanediol, lactic acid, adipic acid, glutamic acid, itaconic acid, ethyl acetate, isopropyl acetate, acetic acid, butyric acid, caproic acid, citric acid, methacrylic acid, succinic acid, propylene, butadiene, ethanol, isoprenol, leucine, isoleucine, glutamine, glycine, and isoprene, from β-alanine. The recombinant microorganism expresses an asparate 1-decarboxylase that catalyzes the production of malonate semialdehyde from β-alanine.

RECOMBINANT YEAST CAPABLE OF PRODUCING CAFFEIC ACID AND/OR FERULIC ACID

The present invention relates to a recombinant microorganism, preferably a recombinant yeast, capable of producing caffeic acid comprising a heterologous gene coding for an enzyme of the hydrolase family capable of breaking, preferably of hydrolyzing, the caffeoyl-shikimate bond to produce caffeic acid from caffeoyl-shikimate. Said microorganism, preferably said recombinant yeast, may also be capable of producing ferulic acid from the caffeic acid obtained. The present invention also relates to a method for producing caffeic acid and a method for producing caffeic acid and/or ferulic acid, using microorganisms, preferably yeasts, according to the invention. Finally, the invention also relates to the use of microorganisms, preferably yeasts, according to the invention to produce caffeic acid and/or ferulic acid.

PRODUCTION OF CHEMICALS FROM RENEWABLE SOURCES

Among other things, the present disclosure provides biosynthesis polypeptides, methods, and non-naturally occurring microbial organisms for preparing various compounds such as 1,5-pentanediol, adipic acid, 1,6-hexanediol, 6-hydroxy hexanoic acid, and 2-keto carboxylic acids.

PRODUCTION OF PYRUVATE OR PRODUCTS DERIVED FROM PYRUVATE USING MODIFIED ESCHERICHIA COLI
20220372451 · 2022-11-24 ·

Modified bacterial strains are provided. The strains can generate a desired product such as pyruvate and products derived from pyruvate. Methods of generating pyruvate and products derived from pyruvate are also provided. The modified bacterial strains have at least one mutation in a gene coding for proteins in a pyruvate dehydrogenase complex such that the mutation allows a cell to accumulate pyruvate and/or products derived from pyruvate.

Method for the preparation of 2,4-dihydroxybutyrate

A method for the preparation of 2,4-dihydroxybutyric acid from homoserine includes a first step of conversion of the primary amino group of homoserine to a carbonyl group to obtain 2-oxo-4-hydroxybutyrate, and a second step of reduction of the obtained 2-oxo-4-hydroxybutyrate (OHB) to 2,4-dihydroxybutyrate.

Method for the preparation of 2,4-dihydroxybutyrate

A method for the preparation of 2,4-dihydroxybutyric acid from homoserine includes a first step of conversion of the primary amino group of homoserine to a carbonyl group to obtain 2-oxo-4-hydroxybutyrate, and a second step of reduction of the obtained 2-oxo-4-hydroxybutyrate (OHB) to 2,4-dihydroxybutyrate.