C12Y206/00

Production of renewable hydrocarbon compositions

Provided herein are processes and microorganisms which utilize both protein hydrolysates and carbohydrates from biomass feedstocks to produce renewable hydrocarbon compositions. Advantages of the disclosed methods may be recognized in fuel blends comprising such hydrocarbon compositions.

Production of renewable hydrocarbon compositions

Provided herein are processes and microorganisms which utilize both protein hydrolysates and carbohydrates from biomass feedstocks to produce renewable hydrocarbon compositions. Advantages of the disclosed methods may be recognized in fuel blends comprising such hydrocarbon compositions.

Type II fatty acid synthesis enzymes in reverse β-oxidation

This disclosure describes enzymes from the type II (a discrete set of enzymes) fatty acid synthesis (FAS) pathway that can be used in combination with thiolases to operate a functional reversal of the -oxidation cycle. A combination of thiolases with one or more of 3-oxoacyl-[acyl-carrier-protein] reductase (FabG, others), 3-hydroxyacyl-[acp] dehydratase (FabA, FabZ, others), and enoyl-[acyl-carrier-protein] reductase (FabI, FabK, FabL, FabV, others) yields a functional reversal of the -oxidation cycle. If only one or two enzymes are used, the remaining enzymes will be traditional beta oxidation enzymes. Once this cycle is coupled with the appropriate priming and termination pathways, the production of carboxylic acids, alcohols, hydrocarbons, amines and their -, -, and -functionalized derivatives from renewable carbon sources can be achieved.

Production of Renewable Hydrocarbon Compositions
20180066290 · 2018-03-08 ·

Provided herein are processes and microorganisms which utilize both protein hydrolysates and carbohydrates from biomass feedstocks to produce renewable hydrocarbon compositions. Advantages of the disclosed methods may be recognized in fuel blends comprising such hydrocarbon compositions.

ENZYMATIC SYNTHESIS OF OPTICALLY ACTIVE CHIRAL AMINES

The present invention relates to a method of enantioselective enzymatic transamination of (1R)-1-Hydroxy-1-Phenylacetone (R-PAC) to a chiral amine 1R, 2S-Norephedrine in the presence of an isopropylamine catalyzed by enantioselective transaminase. Isopropylamine is converted to acetone in the process. The transaminase used is in completely purified form, partially purified form or as whole cells. The source is microbial cells, which are genetically engineered. In the present invention, the enzyme is expressed in E. coli and used preferentially as a suspension of native cells. Transaminase comprising polypeptide sequence is obtained from Rhodobacter sphaeroides and expressed in E. coli. The nucleotide sequence of transaminase is expressed in an expression vector system pIEP/Kan/IEP AT12, which is incorporated in E. coli. The yield of 1R, 2S-1-norephedrine is greater than 87% and de % is greater than 99%. The enantioselective transamination process is cost-effective and environment-friendly in addition to providing the amine in high yield and enantioselectivity.

PRODUCTION OF CHIRAL 1,2-AMINO ALCOHOLS AND ALPHA-AMINO ACIDS FROM ALKENES BY CASCADE BIOCATALYSIS
20170067084 · 2017-03-09 ·

Disclosed herein are methods of forming chiral 1,2-aminoalcohols and -aminoacids from alkene starting materials by way of an enzymatic cascade reaction sequence that may be accomplished in a single reaction vessel without the need to isolate any intermediates. Also disclosed herein are recombinant nucleic acids, vectors and host cells for use in the methods of the invention.