C12Y102/01002

SYNTHETIC METHANOTROPHIC AND METHYLOTROPHIC MICROORGANISMS
20200277636 · 2020-09-03 ·

Provided herein are non-naturally occurring microbial organisms comprising a methane-oxidizing metabolic pathway. The invention additionally comprises non-naturally occurring microbial organisms comprising pathways for the production of chemicals. The invention additionally provides methods for using said organisms for the production of chemicals.

Formate dehydrogenase mutant with improved enzyme activity and stability and construction method thereof

The present invention discloses a formate dehydrogenase mutant with improved enzyme activity and stability and a construction method thereof, which belongs to the technical field of genetic engineering. The mutant of the present invention is obtained by mutating alanine at a 10.sup.th site to cysteine based on the amino acid shown in SEQ ID NO. 2. The specific enzyme activity of the mutant enzyme obtained by the present invention is improved by 1.3 times compared with that before the mutation, a half-life period (t.sub.1/2) at 60 C. is increased by 6.8 times compared with that in the mutation period, the copper ion tolerance is increased by 30 times compared with that before the mutation, and when pH is 4, the stability is improved by 2.0 times, and the catalytic efficiency is increased by 1.4 times. The present invention shows that an amino acid residue at a 10.sup.th site is mutated to the cysteine which forms a correct disulfide bond with a cysteine residue at a 30.sup.th site of the natural formate dehydrogenase, so that the stability and the catalytic efficiency of the enzyme are improved, and the industrial application potential of the enzyme is improved.

Synthetic methanotrophic and methylotrophic microorganism and method thereof

Provided herein are non-naturally occurring microbial organisms comprising a methane-oxidizing metabolic pathway. The invention additionally comprises non-naturally occurring microbial organisms comprising pathways for the production of chemicals. The invention additionally provides methods for using said organisms for the production of chemicals.

MICROORGANISMS AND METHODS FOR PRODUCTION OF SPECIFIC LENGTH FATTY ALCOHOLS AND RELATED COMPOUNDS
20200157585 · 2020-05-21 ·

The invention provides non-naturally occurring microbial organisms containing a fatty alcohol, fatty aldehyde or fatty acid pathway, wherein the microbial organisms selectively produce a fatty alcohol, fatty aldehyde or fatty acid of a specified length. Also provided are non-naturally occurring microbial organisms having a fatty alcohol, fatty aldehyde or fatty acid pathway, wherein the microbial organisms further include an acetyl-CoA pathway. In some aspects, the microbial organisms of the invention have select gene disruptions or enzyme attenuations that increase production of fatty alcohols, fatty aldehydes or fatty acids. The invention additionally provides methods of using the above microbial organisms to produce a fatty alcohol, a fatty aldehyde or a fatty acid.

Multi-enzyme conjugate, method for preparing the same and method for preparing organic compound using the same

The present disclosure relates to a multi-enzyme conjugate, a method for preparing the same and a method for preparing an organic compound using the same. More particularly, a multi-enzyme conjugate exhibiting improved catalytic efficiency over respective free enzymes using site-specific incorporation of a clickable non-natural amino acid into the enzymes and two compatible click reactions, a method for preparing the same and a method for preparing an organic compound using the same may be provided.

Methods of producing 6-carbon chemicals via CoA-dependent carbon chain elongation associated with carbon storage

This document describes biochemical pathways for producing adipic acid, caprolactam, 6-aminohexanoic acid, 6-hydroxyhexanoic acid, hexamethylenediamine or 1,6-hexanediol by forming two terminal functional groups, comprised of carboxyl, amine or hydroxyl groups, in a C6 aliphatic backbone substrate. These pathways, metabolic engineering and cultivation strategies described herein rely on CoA-dependent elongation enzymes or analogues enzymes associated with the carbon storage pathways from polyhydroxyalkanoate accumulating bacteria.

PUTRESCINE-PRODUCING MICROORGANISM AND METHOD FOR PRODUCING PUTRESCINE USING THE SAME

The present application relates to a putrescine-producing microorganism in which the activity of formate dehydrogenase is increased, and a method for producing putrescine using the same.

Microorganisms and methods for production of specific length fatty alcohols and related compounds

The invention provides non-naturally occurring microbial organisms containing a fatty alcohol, fatty aldehyde or fatty acid pathway, wherein the microbial organisms selectively produce a fatty alcohol, fatty aldehyde or fatty acid of a specified length. Also provided are non-naturally occurring microbial organisms having a fatty alcohol, fatty aldehyde or fatty acid pathway, wherein the microbial organisms further include an acetyl-CoA pathway. In some aspects, the microbial organisms of the invention have select gene disruptions or enzyme attenuations that increase production of fatty alcohols, fatty aldehydes or fatty acids. The invention additionally provides methods of using the above microbial organisms to produce a fatty alcohol, a fatty aldehyde or a fatty acid.

Method for producing L-α-amino acid compound
10364448 · 2019-07-30 · ·

Isolated oxidases, isolated polynucleotides encoding the oxidases, and methods of using the oxidases to produce -oxocarboxylic acid compounds or L--amino acid compounds are described.

Formate Dehydrogenase Mutant with Improved Enzyme Activity and Stability and Construction Method thereof

The present invention discloses a formate dehydrogenase mutant with improved enzyme activity and stability and a construction method thereof, which belongs to the technical field of genetic engineering. The mutant of the present invention is obtained by mutating alanine at a 10.sup.th site to cysteine based on the amino acid shown in SEQ ID NO. 2. The specific enzyme activity of the mutant enzyme obtained by the present invention is improved by 1.3 times compared with that before the mutation, a half-life period (t.sub.1/2) at 60 C. is increased by 6.8 times compared with that in the mutation period, the copper ion tolerance is increased by 30 times compared with that before the mutation, and when pH is 4, the stability is improved by 2.0 times, and the catalytic efficiency is increased by 1.4 times. The present invention shows that an amino acid residue at a 10.sup.th site is mutated to the cysteine which forms a correct disulfide bond with a cysteine residue at a 30.sup.th site of the natural formate dehydrogenase, so that the stability and the catalytic efficiency of the enzyme are improved, and the industrial application potential of the enzyme is improved.