C12P13/001

Biocatalysts for the preparation of hydroxy substituted carbamates

The present disclosure relates to engineered ketoreductase polypeptides for the preparation of hydroxyl substituted carbamate compounds, and polynucleotides, vectors, host cells, and methods of making and using the ketoreductase polypeptides.

Coryneform bacterium transformant with improved aniline productivity and process for producing aniline using the same

An objective of the present invention is to provide a microorganism capable of efficiently producing aniline from aminobenzoic acid, and a process for efficiently producing aniline from aminobenzoic acid. To achieve the objective, provided is an aniline-producing transformant constructed by introducing a gene which encodes an enzyme having aminobenzoate decarboxylase activity into a coryneform bacterium as a host, characterized in that the enzyme having aminobenzoate decarboxylase activity is composed of an amino acid sequence which is the same as that represented by SEQ ID NO: 2 except for having a mutation of at least proline (P) at position 309 from the N terminus.

TYROSINE HYDROXYLASE VARIANTS AND METHODS OF USE THEREOF

The present disclosure provides a variant tyrosine hydroxylase that provides for increased production of L-DOPA in a host cell that expresses the tyrosine hydroxylase. The present disclosure provides nucleic acids encoding the variant tyrosine hydroxylase, and host cells genetically modified with the nucleic acids. The present disclosure provides methods of making L-DOPA in a host cell. The present disclosure provides methods of making a benzylisoquinoline alkaloid (BIA), or a BIA precursor. The present disclosure provides methods of detecting L-DOPA level in a cell. The present disclosure provides methods of identifying tyrosine hydroxylase variants that provide for increased L-DOPA production; and methods of identifying gene products that provide for increased tyrosine production.

PROCESS FOR THE PREPARATION OF DROXIDOPA

A novel process for the preparation of L-threo-dihydroxyphenylserine (Droxidopa) is described. It comprises of enantioselective hydrolysis of racemic (DL)-threo-N-acetyl-3-(3,4-methylenedioxyphenyl)-serine using commercially available L-amino acylase from Aspergillus sp. (EC 3.5.1.14) in the presence of cobalt ions, to obtain (L)-threo-3-(3,4-methylenedioxyphenyl)-serine followed by dealkylation to obtain Droxidopa. Protecting the amino group of (L)-threo-3-(3,4-methylenedioxyphenyl)-serine using either benzyloxycarbonyl or phthaloyl group before dealkylation followed by deprotection of the amino group results in obtaining Droxidopa in high yields and purity.

Methods of producing 7-carbon chemicals via CoA-dependent carbon chain elongation associated with carbon storage

This document describes biochemical pathways for producing pimelic acid, 7-hydroxyheptanoic acid, 7-aminoheptanoic acid, heptamethylenediamine or 1,7-heptanediol by forming two terminal functional groups, comprised of carboxyl, amine or hydroxyl group, in a C7 aliphatic backbone substrate. These pathways, metabolic engineering and cultivation strategies described herein rely on the CoA-dependent elongation enzymes or analog enzymes associated with the carbon storage pathways from polyhydroxyalkanoate accumulating bacteria.

VARIANT MICROORGANISM PRODUCING 5-AMINOLEVULINIC ACID AND METHOD FOR PREPARING 5-AMINOLEVULINIC ACID USING THEREOF
20170292134 · 2017-10-12 ·

The present invention relates to a mutant microorganism having the ability to produce 5-aminolevulinic acid, and more particularly, to a mutant microorganism having the ability to produce 5-aminolevulinic acid wherein a glutamyl-tRNA reductase-encoding gene is introduced in a glutamic acid-producing microorganism, and to a method for producing 5-aminolevulinic acid using the same. According to the present invention, 5-aminolevulinic acid that is useful in the medical or agricultural field can be produced in a significantly higher yield than that of conventional production methods.

Biocatalytic methods to convert cyclohexane oxidation process waste streams to useful products

The invention relates to methods for enriching monomer content in a cycloalkane oxidation process mixed organic waste stream. In particular, the methods involve combining a biocatalyst with a mixed organic waste stream from a cycloalkane oxidation process, and enzymatically converting dimeric and/or oligomeric components of said waste stream into monomeric components. The methods may enrich the content of diacids, adipic acid, and/or other α,ω-difunctional C6 alkanes in the mixed organic waste stream. Additionally, the treated mixed organic waste streams may have improved burning efficiency.

Catecholamine-based versatility film and a preparation method thereof

The present invention relates to a method for preparing a double-sided film containing the step of 5 forming a film in the interface between air and the mixture of a polymer comprising amine group (—NH) and a compound containing phenol or catechol by exposing the mixture on the air. Particularly, the double-sided film of the present invention is a separation membrane 10 that can separate the interface of liquid phase and gas phase and at the same time can be used as a biomaterial such as a haemostatic and also an waterproof agent. When the film is prepared in a moderate condition by using an enzyme, the film can include proteins and 15 cells, resulting in the multi-functional versatility film that can be useful as a biocatalyst. The versatility film of the present invention, thus, is not expensive and the production method thereof is simple and eco-friendly.

MODIFICATIONS OF SOLID 3-SN-PHOSPHOGLYCERIDES

Methods for hydrolyzing solid ungranulated lysophosphatidylcholine with phospholipase A.sub.2 are provided. Also disclosed are methods for making a lipid matrix of lysophosphatidylcholine, monoglyceride and fatty acid, and lipid matrices of particular structure.

Method for producing optically active amine compounds by deracemization

Disclosed are methods for producing optically active amino acids and amines. According to the methods, α-keto acids are generated as reaction intermediates, and as a result, ω-transaminase-catalyzed kinetic resolution of racemic amino acids or amines as racemic amine compounds enables the production of optically active amine compounds without the need to use expensive α-keto acids as starting materials. Therefore, the optically active amine compounds are produced at greatly reduced costs. In addition, the optically active amine compounds have high enantiomeric excess.