A method for producing a chiral amine may include performing a transamination reaction of a prochiral amino acceptor and an amino donor in a first solution in the presence of a transaminase, thereby forming a chiral amine and a co-product in the first solution. The amino donor is a high molecular weight (HMW) amino donor. In some examples, the molecular weight of the HMW amino donor is at least 150 g/mol. In some examples, the amino donor is affixed on a support, the total molecular weight of the amino donor and the support being at least 150 g/mol.

Disclosed is a recombinant microorganism capable of growing using only carbon dioxide and formic acid by introducing and improving a metabolic pathway for synthesizing pyruvic acid from carbon dioxide and formic acid to enhance pyruvic acid synthesis efficiency and performing additional genetic manipulation, and a method for producing useful substances using the same. Advantageously, the recombinant microorganism is capable of synthesizing pyruvic acid, a C3 organic compound, at a remarkably improved rate, and in particular, grows well even in a medium containing only carbon dioxide and formic acid as carbon sources without a glucose supply, and is thereby capable of synthesizing pyruvic acid and various high value-added compounds using the same as an intermediate product in an economically efficient manner.

The present invention provides at least two modified gene sequences, Sequence 1 comprising of nucleotide sequence of SEQ. ID no.1, and Sequence 2 comprising of nucleotide sequence of SEQ. ID no.2, encoding the enzyme choline oxidase wherein the gene sequences have been obtained by modifying the codA gene (Accession no. X84895) encoding choline oxidase from Arthrobacter globiformis, and a method to enzymatically produce betaine using choline oxidases encoded by Sequence 1, and Sequence 2, wherein the enzymatically produced betaine has minimal undesired trimethylamine contamination.

The present invention describes an approach to produce or increase hypotaurine or taurine production in unicellular organisms. More particularly, the invention relates to genetic modification of unicellular organisms that include bacteria, algal, microalgal, diatoms, yeast, or fungi. The invention relates to methods to increase taurine levels in the cells by binding taurine or decreasing taurine degradation. The invention can be used in organisms that contain native or heterologous (transgenic) taurine biosynthetic pathways or cells that have taurine by enrichment. The invention also relates to methods to increase taurine levels in the cells and to use the said cells or extracts or purifications from the cells that contain the invention to produce plant growth enhancers, food, animal feed, aquafeed, food or drink supplements, animal-feed supplements, dietary supplements, health supplements or taurine.

An R-3-aminobutyric acid preparation method with high efficiency and high stereoselectivity. The method comprises using aspartase with stereoisomerization catalytic activity derived from Escherichia coli to efficiently convert butenoic acid into R-3-aminobutyric acid. After only 24 h of reaction, the conversion rate is as high as ≥98%, and the ee value is ≥99.9%. The conversion efficiency is greatly improved, the reaction time is shortened, and the production costs are reduced. The method features a high yield, a high conversion rate, low costs, a short production cycle, a simple process, ease of enlargement, suitability for mass production and the like.

The present disclosure provides engineered transaminase polypeptides useful for the synthesis of chiral amine compounds under industrially relevant conditions. The disclosure also provides polynucleotides encoding the engineered transaminase polypeptides, host cells capable of expressing the engineered transaminases, and methods of using the engineered transaminases for the production of chiral amine compounds.

The present invention relates to a process for preparing ammonium (meth-) acrylate, aqueous ammonium (meth-) acrylate solutions obtainable by such process, and (meth-) acrylic acid homopolymers or copolymers obtainable by polymerizing such ammonium (meth-) acrylate. The invention furthermore relates to a modular, relocatable bioconversion unit for manufacturing aqueous ammonium (meth-) acrylate solutions.

The present invention relates generally to an eco-friendly methodology for the conversion of alcohols and aldehydes to amines and amides using an integrated enzyme cascade system with metal- and organocatalysis. More specifically, the present invention relates to synthesis of capsaicinoids starting from vanillin alcohol and using a combination of an enzyme cascade system and catalysts. Furthermore, the method also relates to synthesis of capsaicinoids derivatives starting from vanillin alcohol derivatives and using a combination of an enzyme cascade system and catalysts.

The invention relates to a method for producing aminobenzoic acid or a aminobenzoic acid derivative via the fermentation of a suitable raw material under the influence of suitable microorganisms and obtaining a fermentation broth containing aminobenzoate and/or aminobenzoic acid. In particular, the invention relates to the step of obtaining the aminobenzoic acid from the fermentation broth, wherein the crystallisation of aminobenzoic acid is carried out via a simple one-stage acid treatment in the presence of seed crystals. The aminobenzoic acid crystallised in this simple manner can be easily separated from the mother liquor, further cleaned if necessary, and then supplied to the different applications.

Provided are a method for obtaining an HNL gene and HNL derived from a millipede other than Chamberlinius hualienensis, and preparing a practically useable amount of HNL; and a method for producing optically active cyanohydrin using this HNL. A method for producing a millipede-derived HNL gene. A method that includes the selection of a gene having a base sequence that encodes a conserved amino acid sequence TAX1DIX2G (SEQ ID NO: 15) or VPNGDKIH (SEQ ID NO: 16) of millipede-derived HNL from genes present in an organism belonging to the Diplopoda. A protein having an amino acid sequence of any of (1)-(3) and having HNL activity. (1) An amino acid sequence listed in any of SEQ ID NOS: 1, 3, 5, 7, 9, 11, 13, 83, 85, 87, or 89; (2) an amino acid sequence having amino acids deleted, substituted, and/or added in an amino acid sequence of (1); or (3) an amino acid sequence having 90% or greater identity to an amino acid sequence of (1). A method for preparing optically active cyanohydrin by causing this millipede-derived HNL to act on a reaction solvent that contains an aldehyde or the like and a substance that generates hydrogen cyanide or the like.