Abstract: This invention is intended to improve glutathione productivity by fermentation using microorganisms. This invention relates to a microbial strain capable of overexpression of ?-glutamylcysteine, bis-?-glutamylcystine, ?-glutamylcystine, reduced glutathione, and/or oxidized glutathione in which the expression level of a gene encoding serine-O-acetyltransferase (EC:2.3.1.30) is enhanced and a method involving the use of such microbial strain.

Abstract: The present disclosure concerns a method for producing peptides such as glutathione and a microorganism that can be used for such method. One or more embodiments of the first aspect of the present disclosure concern a method for producing peptides such as glutathione comprising culturing a prokaryotic microbial strain in which the expression levels of one or more genes selected from among the gshA gene, the gshB gene, and the gshF gene are enhanced, compared with the expression levels thereof in the wild-type strain thereof in a medium in which the total concentration of cysteine and cystine is 0.5 g/l or lower. The second aspect of the present disclosure concerns a microorganism comprising disruptions of the ?-glutamyltransferase gene and the glutathione reductase gene and exhibiting the enhanced expression levels of the gshA gene and the gshB or gshF gene.

Abstract: A method of producing a substance includes synthesizing a molecule at least by mixing substrates, a synthase, adenosine triphosphate (ATP), a polyphosphate kinase 2, and a polyphosphoric acid mixture. The polyphosphoric acid mixture includes 50% or more of polyphosphoric acid with a degree of polymerization of not less than 15. Adenosine diphosphate (ADP) is generated from the ATP during the synthesis. The synthesis is coupled with an ATP regeneration reaction in which the ATP is regenerated by the polyphosphate kinase 2 from the ADP and the polyphosphoric acid.

Abstract: A polypeptide includes a mutant sequence of the amino acid sequence of SEQ ID NO: The mutant sequence includes one or more amino acid substitutions in the amino acid sequence of SEQ ID NO: 1 at positions 13, 17, 20, 23, 39, 70, 78, 101, 113, 125, 126, 136, 138, 149, 152, 154, 155, 197, 200, 215, 226, 227, 230, 239, 241, 246, 249, 254, 260, 262, 263, 270, 278, 299, 305, 307, and 310. The mutant sequence may further include one or more amino acid substitutions, additions, insertions, or deletions. The mutant sequence, excluding the substituted residue(s), may have a sequence identity of 80% or more with the amino acid sequence of SEQ ID NO: 1.

Abstract: An object of the present invention is to modify a wild-type enzyme that is less reactive in the presence of an organic solvent to provide altered carbonyl reductases having better reactivity in the presence of the organic solvent than the wild-type enzyme, and/or to provide transformants producing such reductases. The present inventors have found altered carbonyl reductases having better reactivity in the presence of an organic solvent than the wild-type enzyme, from among a mutant enzyme library prepared by randomly mutating the wild-type enzyme gene, thereby arriving at completion of the present invention.

Abstract: An object of the present invention is to modify a wild-type enzyme that is less reactive in the presence of an organic solvent to provide altered carbonyl reductases having better reactivity in the presence of the organic solvent than the wild-type enzyme, and/or to provide transformants producing such reductases. The present inventors have found altered carbonyl reductases having better reactivity in the presence of an organic solvent than the wild-type enzyme, from among a mutant enzyme library prepared by randomly mutating the wild-type enzyme gene, thereby arriving at completion of the present invention.