Abstract: The invention relates to the directed evolution of CYP52A12 gene and the use thereof for the production of a dicarboxylic acid. In particular, it relates to a method of preparing a long chain dicarboxylic acid producing strain by using directed evolution and homologous recombination, a strain obtained by the method that is capable of producing a long chain dicarboxylic acid under an acidic condition and the use thereof. In particular, the invention relates to a method of preparing a long chain dicarboxylic acid producing strain by directed evolution of CYP52A12 gene and homologous recombination, a strain obtained by the method that is capable of producing a long chain dicarboxylic acid under an acidic condition and the use thereof. By directed evolution of CYP52A12 gene, one strain which has a base mutation at the promoter region of said gene and is capable of producing a long chain dicarboxylic acid under an acidic condition in a shortened fermentation time is screened out in the invention.

Abstract: It is an object of the present invention to provide a novel enzyme useful for producing low-purine foods or beverages. There is disclosed a nucleosidase comprising an amino acid sequence of SEQ ID NO: 1 or an amino acid sequence having 85% or more identity with the amino acid sequence, or an amino acid sequence of SEQ ID NO: 2 or an amino acid sequence having 88% or more identity with the amino acid sequence.

Abstract: An isolated and/or purified ?-glucanotransferase from Exiguobacterium Acetylicum, recombinantly engineered variants thereof, active fragments thereof, synthetic nucleic acids encoding the ?-glucanotransferase and variants thereof, host cells comprising the synthetic nucleic acids, and compositions comprising the ?-glucanotransferase are provided. Methods of using the compositions include the manufacture of oligosaccharides.

Abstract: The present invention discloses a method for producing a 1,2-amino alcohol compound by utilizing whole-cell transformation, and belongs to the technical field of gene engineering and microorganism engineering. According to the present invention, engineered Escherichia coli co-expresses epoxide hydrolase, alcohol dehydrogenase, ?-transaminase and glutamate dehydrogenase, is capable of realizing whole-cell catalysis of an epoxide in one step to synthesize a 1,2-amino alcohol compound, and meanwhile, can realize regeneration of coenzyme NADP+ and an amino doner L-Glu; alcohol dehydrogenase expressed by the engineered Escherichia coli is RBS optimized alcohol dehydrogenase, and such RBS optimization can control the expression quantity of alcohol dehydrogenase, so that the catalysis rate of alcohol dehydrogenase and transaminase can achieve an optimum ratio, to eliminate influence caused by a rate-limiting step in a catalyzing course.

Abstract: The present invention relates to a new process of vanillin production from a substrate by bioconversion and that allows a continuously producing and removing vanillin from the fermentation broth as it is formed. In particular, the invented process advantageously allows to reduce the residence time of vanillin in the fermenter and to maintain the vanillin concentration, in the fermentation broth, below its toxic level for the microorganism.

Abstract: The present invention relates to a modified yeast strain of Saccharomyces cerevisiae having MCC accession number 0069 with osmo-tolerant, thermo-tolerant, ethanol tolerant and self-flocculation properties. Further, the present invention relates to a method for obtaining modified yeast strain. The present invention also relates to a method of production of ethanol at high temperature using said yeast strain. The ethanol produced by the method disclosed in the present invention is used as fuel.

Abstract: A modified transferrin DNA binding domain. The transferrin is lactotransferrin (LTF), serotransferrin (TF), melanotransferrin (MTF) or ovotransferrin (OTF), and the N terminal of each transferrin has one homologous DNA binding domain, wherein the 10th site and 20th site of the DNA binding domain are C; and the amino acid sequence of the modified transferrin DNA binding domain is as follows: C in the 10th site and 20th? site is replaced by other amino acids so that no disulfide bond can be formed. The present invention also discloses a recombinant DNA polymerase and a preparation method thereof. The preparation method comprises the step of coupling the modified transferrin DNA binding domain with a DNA polymerase. The present invention also discloses a PCR test kit containing the recombinant DNA polymerase.

Abstract: The present disclosure relates to detergent compositions comprising polypeptides having xanthan degrading activity. The disclosure also relates to methods for producing said detergent compositions and to the use of said detergent compositions in cleaning applications.

Abstract: Polypeptides comprising maltose/maltotriose transporters are provided. Additionally, polynucleotides, DNA constructs, and vectors encoding a maltose/maltotriose transporter, or yeast cells harboring such polynucleotides are provided. The yeast cell may be a Saccharomyces eubayanus cell modified to increase the expression or transport activity of a maltose/maltotriose transporter at the plasma membrane of the cell. Further, methods are provided for making a fermentation product by culturing any one of the yeast cells described herein with a fermentable substrate. Finally, methods are provided to select for and isolate maltotriose-utilizing strains of Saccharomyces eubayanus.

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: The present invention relates to novel mutant thioesterase enzymes and naturally-occurring equivalents thereof, compositions made from such enzymes and uses of thioesterase enzymes. In particular, the present invention provides mutant thioesterase enzymes that have altered properties, for example, altered substrate specificity, altered activity, altered selectivity, and/or altered proportional yields in the product mixtures. The present invention also provides polynucleotides encoding such mutant thioesterase enzymes, and vectors and host cells comprising such polynucleotides. The invention further provides for novel uses of thioesterases in the production of various fatty acid derivatives, which are useful as, or as components of, industrial chemicals and fuels.

Abstract: The invention is in the field of protein chemistry, in particular in the field of enzymology. It provides pectinases, i.e. polypeptides with pectin-degrading properties. In particular the invention provides polypeptides with pectate lyase activity (EC 4.2.2.2). Enzymes according to the invention have improved properties, such as improved thermostability and decreased calcium dependence.

Abstract: The present disclosure relates to detergent compositions comprising xanthan lyase variants and methods for use of said compositions.

Abstract: The present invention discloses a nitrilase mutant and application thereof. The mutant is obtained by mutating the amino acid at position 201 or replacing one or more amino acids at region 324-381 of the amino acid sequence shown in SEQ ID No. 2. In the present invention, by the protein molecular modification, thermostability of the purified nitrilase LNIT5 is increased by up to 4.5 folds; and by utilizing recombinant E. coli containing the nitrilase mutant to hydrolyze 1-cyanocyclohexylacetonitrile at a high temperature (45° C.), product tolerance is increased, activity of NIT5-L201F is increased by 20%, and the mutant NITLNIT5-AcN can completely hydrolyze 750 mM 1-cyanocyclohexylacetonitrile within 8 hours and achieve an doubled conversion rate. Therefore, the mutants obtained by the present invention have a good application prospect in efficiently catalyzing 1-cyanocyclohexylacetonitrile to synthesize gabapentin intermediate, 1-cyanocyclohexyl acetic acid.

Abstract: The present invention provides engineered phenylalanine ammonia lyase (PAL) polypeptides and compositions thereof, as well as polynucleotides encoding the engineered phenylalanine ammonia lyase (PAL) polypeptides. In some embodiments, the engineered PAL polypeptides are optimized to provide enhanced catalytic activity, as well as reduced sensitivity to proteolysis and increased tolerance to storage at elevated temperatures. In some embodiments, the engineered PAL polypeptides contain fewer phenylalanine residues than wild-type PAL polypeptides. The present invention also provides methods for the use of the compositions comprising the engineered PAL polypeptides for therapeutic and industrial purposes.

Abstract: The present disclosure relates to a detergent composition comprising endoglucanase variants and methods for use of said compositions.

Abstract: Provided is a microorganism that is capable of efficiently producing para-aminobenzoic acid (4-ABA) or a salt thereof, using saccharides as raw materials, and a method for efficiently producing 4-ABA or a salt thereof by using this microorganism. A transformant obtained by introducing, into a coryneform bacterium, a gene that encodes 4-amino-4-deoxychorismate lyase, a gene that encodes a para-aminobenzoate synthase component I, and a gene that encodes a para-aminobenzoate synthase component II, is capable of efficiently producing 4-ABA or a salt thereof from saccharides.

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

Abstract: The present invention relates to a process for the microbial in-chain hydroxylation of C12 to C16 fatty acids, alcohols and alkanes at position ?-7, the process including the use of a microorganism expressing a cytochrome P450 monooxygenase CYP505E3 or related fungal cytochrome P450 monooxygenases sharing at least 70% amino acid identity in the production of a hydroxylated product or secondary product. The present invention further relates to a process for the preparation of lactones, esters and polymers by hydroxylation of the corresponding fatty acids, fatty alcohols and alkane precursors by a recombinant cytochrome P450 monooxygenase CYP505E3 or related fungal cytochrome P450 monooxygenases sharing at least 70% amino acid identity.

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).