Provided is a method for producing 1,3-propanediol by means of fermentation of a recombinant microorganism. First, a recombinant microorganism is provided; the recombinant microorganism can overexpress acetyl-CoA carboxylase genes: accBC and accDA, a malonyl-CoA synthetase gene: mcr, a 3-hydroxypropionyl-CoA synthetase gene: pcs, a 3-hydroxypropionyl-CoA reductase gene: pduP, and a 1,3-propanediol reductase gene: yqhD. The recombinant microorganism is subjected to fermentation culture in a flask or fermentor using glucose ad as raw material to obtain the 1,3-propanediol. The recombinant microorganism can utilize low-cost glucose, sucrose, molasses, xylose and the like as raw material in the fermentation process, without additional expensive vitamin B12. Thus, cost of the production is significantly reduced, and there is a promising prospect in market.

The invention discloses an alcohol dehydrogenase mutant and use thereof. The alcohol dehydrogenase mutant of the present invention has high thermal stability and enables high catalytic efficiency and high conversion rate (i.e. space time yield) in the asymmetric reduction of prochiral diaryl ketones to produce chiral diaryl alcohols. Therefore, the alcohol dehydrogenase mutant of the present invention has extremely high prospect of application in the production of chiral diaryl alcohols, such as (S)-(4-chlorophenyl)-(pyridin-2-yl)-methanol, (R)-(4-chlorophenyl)-(pyridin-2-yl)-methanol.

Provided herein is a non-naturally occurring microbial organism (NNOMO) having a methanol metabolic pathway (MMP) that can enhance the availability of reducing equivalents in the presence of methanol. Such reducing equivalents can be used to increase the product yield of organic compounds produced by the microbial organism, such as succinate. Also provided herein are methods for using such an organism to produce succinate.

The present disclosure provides microbial organisms having increased availability of co-factors, such as NADPH, for increasing production of various products, including 1,3-BDO, MMA, (3R)-hydroxybutyl (3R)-hydroxybutyrate, amino acids, 3HB-CoA, adipate, caprolactam, 6-ACA, HMD A, or MAA, and products made from any of these. Also provided are one or more exogenous nucleic acids encoding an enzyme expressed in a sufficient amount to increase availability of NADPH, where the exogenous nucleic acid includes one or more of ATP-NADH kinase, pntAB, nadK, and gapN. Also provided are one or more gene attenuations occurring in genes, such as NDH-2, that result in an increased ratio of NADPH to NADH. Various combinations of the exogenous nucleic acids and gene deletions are also provided in the present disclosure. The present disclosure also provides methods of making and using the same, including methods for culturing cells, and for the production of the various products.

Disclosed are a ketoreductase mutant and a method for producing a chiral alcohol. The ketoreductase mutant has an amino acid sequence obtained by the mutation of the amino acid sequence shown in SEQ ID NO: 1, and the mutation includes a mutation siteK200H. In the present disclosure, the mutant obtained by mutation takes a ketone compound as a raw material, the chiral alcohol may be efficiently produced by stereoselective reduction, and the stability is greatly improved, which is suitable for popularization and application to the industrial production of the chiral alcohol.

The invention provides lipid bodies isolated from yeast, compositions comprising the lipid bodies, products made from the lipid bodies, methods of making the lipid bodies, and methods of using the lipid bodies. The lipid bodies of the invention have an exceptionally large size and high internal neutral lipid content, providing a number of advantages for a variety of practical applications.

The present disclosure relates to biological processes and systems for the production of isopropanol and/or acetone utilizing modified alcohol dehydrogenases that exhibit increased activity with NADH as a cofactor. The disclosure further relates to polynucleotides and polypeptides of the modified alcohol dehydrogenases, and host cells containing the polynucleotides and expressing the polypeptides.

Provided are a microorganism that produces a diamine compound and a method of producing a diamine compound.

The genetically modified microorganism expresses an enzyme involved in synthesis of a diamine compound, in which the diamine compound is represented by Formula: H.sub.2N—R—NH.sub.2 (wherein, R is a chain or cyclic organic group comprised of one or more atoms selected from the group consisting of C, H, O, N, and S), and the genetically modified microorganism is modified to reduce an activity of an alcohol dehydrogenase compared to a non-reduced strain.

Provided is a method for measuring pentosidine in a specimen, the measurement method comprising the steps of: degrading the specimen with an amino acid degrading enzyme; contacting the specimen after the degradation step with a protein having activity that oxidatively degrades pentosidine; and detecting change resulting from the contact, wherein the amino acid degrading enzyme and the protein having activity that oxidatively degrades pentosidine are different from each other.

By using a mutant glucose oxidase comprising an amino acid sequence in which a residue corresponding to isoleucine at position 489 or arginine at position 335 in the amino acid sequence of SEQ ID NO:1 is substituted with an amino acid residue having a reactive functional group in a side chain, and binding an electron acceptor to the mutant glucose oxidase through the amino acid residue having a reactive functional group, an electron acceptor-modified glucose oxidase is obtained.