Abstract: The present disclosure relates to a microorganism expressing active D-proline reductase.

Abstract: A recombinant filamentous fungi that includes reduced 2-Keto-3-Deoxy-Gluconate (KDG) aldolase enzyme activity as compared to the filamentous fungi not transformed to have reduced KDG aldolase enzyme activity is provided. Also provided is a method of producing KDG.

Abstract: The invention relates to cells which make rhamnolipids and are genetically modified such that they have a decreased activity, compared to the wild type thereof, of a glucose dehydrogenase and to a method for producing rhamnolipids using the cells according to the invention.

Abstract: Described herein are prenyltransferases including non-natural variants thereof having at least one amino acid substitution as compared to its corresponding natural or unmodified prenyltransferases and that are capable of at least two-fold greater rate of formation of cannabinoids such as cannabigerolic acid, cannabigerovarinic acid, cannabigerorcinic acid, and cannabigerol, as compared to a wild type control. Prenyltransferase variants also demonstrated regioselectivity to desired cannabinoid isomers such as CDBA (3-GOLA), 3-GDVA, 3-GOSA, and CBG (2-GOL). The prenyltransferase variants can be used to form prenylated aromatic compounds, and can be expressed in an engineered microbe having a pathway to such compounds, which include 3-GOLA, 3-GDVA, 3-GOSA, and CBG. 3-GOLA can be used for the preparation of cannabigerol (CBG), which can be used in therapeutic compositions.

Abstract: A technique of using a compositional innovation of a dry enzyme composition to improve the stability of a protein deamidase composition enables improvement of the stability of a dry protein deamidase composition by making both a protein deamidase and magnesium chloride coexist in a dry enzyme composition. The technique involves making adjustments so that the pH is at least 2 and less than 5 when the composition is dissolved in water at a concentration of 1 w/v %.

Abstract: A method for producing insoluble alpha-1,3-glucan is disclosed. Embodiments of the method comprise providing (i) oligosaccharides that comprise alpha-1,3 and alpha-1,6 glycosidic linkages, or (ii) oligosaccharides derived from a glucosyltransferase reaction; and contacting at least water, sucrose, a glucosyltransferase enzyme, and the oligosaccharides provided in the first step. Glucosyltransferase reaction compositions embodying such a method, and insoluble products thereof, are also disclosed. Yield and other product benefits can be realized when practicing the disclosed subject matter.

Abstract: A method for the recombinant production of cannabigerolic acid in a host organism may use a modified prenyltransferase. A modified prenyltransferase, a nucleic acid molecule that codes for the modified prenyltransferase, and a recombinant organism that includes the modified prenyltransferase and/or the nucleic acid are also disclosed here.

Abstract: Phosphoethanolamine cellulose and methods of making and using it are disclosed. In particular, the invention relates to a method of producing a phosphoethanolamine cellulose biosynthetically using a BcsG phosphoethanolamine transferase for cellulose modification. Recombinant constructs encoding BcsG are described, including constructs encoding BcsG by itself or in combination with BcsE and BcsF, which increase the extent of cellulose modification and the amount of modified cellulose produced. Production of phosphoethanolamine cellulose in cell culture and derivatization of phosphoethanolamine cellulose are also described.

Abstract: Provided is a D-amino acid oxidative enzyme mutant. The sequence of the mutant comprises a sequence by mutating the 54th amino acid residue N, the 58th amino acid residue F, the 211th amino acid residue C, and the 213th amino acid residue M of the sequence shown in SEQ ID NO:1 or the sequence having at least 76% identity with SEQ ID NO:1. The D-amino acid oxidative enzyme mutant has a higher enzyme activity, enzyme activity stability and/or ammonium resistance than a mild D-amino acid oxidative enzyme mutant. Also provided is an application of the D-amino acid oxidative enzyme mutant in preparing 2-oxo-4-(hydroxymethylphosphinyl)butyric acid.

Abstract: The invention relates to recombinant microorganisms and methods for producing macrocyclic ketones and macrocyclic ketone precursors.

Abstract: The present invention provides use of a manganese peroxidase in the detoxification of mycotoxins, and specifically, the present invention provides five manganese peroxidases (MnP-1, MnP-2, MnP-4, MnP-5, and MnP-6), genes thereof, and uses thereof. The present invention provides five manganese peroxidases (MnP-1, MnP-2, MnP-4, MnP-5, and MnP-6) derived from lignocellulose degradation bacteria, the amino acid sequences thereof being as set forth in SEQ ID NO: 1, SEQ ID NO: 4, SEQ ID NO: 7, SEQ ID NO: 10, and SEQ ID NO: 13.

Abstract: The present invention includes mutant AID, APOBEC, and Tet enzymes with improved functions. In one aspect the invention provides APOBEC fusion proteins comprising hyperactive deamination activity. In another aspect, the invention provides AID mutant proteins comprising hyperactive deamination activity. In yet another aspect, the invention provides mutant Tet proteins capable of stalling oxidation at a 5-hydroxymethylcytosine (hmC).

Abstract: Variants of chymosin with improved milk-clotting properties are disclosed.

Abstract: The purpose of the present invention is to provide a method for producing selenoneine that allows production of selenoneine at higher yields as compared with a conventional technology, and, therefore, enables selenoneine production on an industrial scale. This purpose can be achieved by a method for producing selenoneine, comprising the step of applying histidine and a selenium compound to a transformant that has a gene encoding an enzyme of (1) below introduced therein and that can overexpress the introduced gene, to obtain selenoneine. (1) An enzyme that catalyzes a reaction in which hercynylselenocysteine is produced from histidine and selenocysteine in the presence of S-adenosylmethionine and iron (II).

Abstract: Detergent compositions may include endoglucanase variants and methods of using such detergent compositions. The endoglucanase may have an alteration at one or more positions where the variant has at least 60% but less than 100% sequence identity to SEQ ID NO: 2.

Abstract: A mutant strain of a filamentous fungus of the genus Trichoderma having a reduced function of a polypeptide consisting of the amino acid sequence represented by SEQ ID NO: 2; and a method of producing a sugar from a cellulose-containing biomass, the method including: step a of producing a cellulase by cultivating a Trichoderma reesei mutant strain having a reduced function of a polypeptide consisting of the amino acid sequence represented by SEQ ID NO: 2, and step b of saccharifying the biomass by using the cellulase obtained in the step a.

Abstract: Disclosed herein are oxalate inducing enzymes with pH and thermal stability and methods of using for oxalate related conditions for in food processing.

Abstract: A novel method of producing high-purity hydroxy-L-pipecolic acids in an efficient and inexpensive manner while suppressing the production of hydroxy-L-proline is provided. The method includes allowing an L-pipecolic acid hydroxylase, a microorganism or cell having the ability to produce the enzyme, a processed product of the microorganism or cell, and/or a culture liquid comprising the enzyme and obtained by culturing the microorganism or cell, to act on L-pipecolic acid as a substrate in the presence of 2-oxoglutaric acid and ferrous ion, wherein the L-pipecolic acid hydroxylase has the properties: (1) the enzyme can act on L-pipecolic acid in the presence of 2-oxoglutaric acid and ferrous ion to add a hydroxy group to the carbon atom at positions 3, 4, and/or 5 of L-pipecolic acid; and (2) the enzyme has a catalytic efficiency (kcat/Km) with L-proline that is equal to or less than 7 times the catalytic efficiency (kcat/Km) with L-pipecolic acid.

Abstract: The present invention relates to subtilase variants suitable for use in, e.g., cleaning or detergent compositions, such as laundry detergent compositions and dish wash compositions, including automatic dish wash compositions. The present invention also relates to isolated DNA sequences encoding the variants, expression vectors, host cells, and methods for producing and using the variants of the invention.

Abstract: A method for manufacturing a fermentation product by culturing a microorganism, the method containing steps (A) to (D): (A) culturing the microorganism with a first culture medium; (B) passing a culture solution containing cultured bacterial cells, raw materials for culture, and the fermentation product through an adsorption tower packed with an adsorbent capable of adsorbing the fermentation product from the culture solution, and then collecting an effluent containing the bacterial cells and the raw materials for culture flowing out from the adsorption tower, wherein a relationship among a size (short diameter) d of the bacterial cell, a pore size D1 of the adsorbent, and a minimum void size D2 between adsorbent particles, D1<d<D2 is satisfied; (C) eluting the fermentation product from the absorbent; and (D) culturing the microorganism with a second culture medium using collected effluent containing the bacterial cells and the raw materials for culture.