Abstract: A method for preparing troxerutin ester using whole-cell catalysis belongs to the fields of biological catalysis and pharmaceutical chemistry. The method specifically includes the following steps: evenly mixing troxerutin and a mixed organic solvent containing pyridine, then adding an acyl donor and a whole-cell catalyst, and performing a reaction under oscillation at a reaction temperature of 25° C. to 55° C.; and after the reaction is finished, separating and purifying a product by column chromatography or thin-layer chromatography, so as to obtain the troxerutin ester. The invention has the advantages of mild reaction conditions, environmental friendliness, simple process, fewer side reactions and high selectivity.

Abstract: The present invention provides improved P450-BM3 variants with improved activity. In some embodiments, the P450-BM3 variants exhibit improved activity over a wide range of substrates.

Abstract: The invention is in the field of enzymology. More in particular, it provides a method for the isomerization of glucose into fructose wherein the glucose is derived from lignocellulosic material. More in particular, the invention provides polypeptides encoding mutant glucose isomerase enzymes with improved glucose isomerase activity as compared to the corresponding wild type enzyme. The disclosed polypeptides are particularly suited for converting glucose to fructose in the presence of xylose.

Abstract: The present disclosure provides modified proteins that are capable of being cleaved by the protease OmpT1. The proteins can be modified in an exposed surface motif to incorporate OmpT1 cleavage sites. Also provided are nucleic acids encoding the modified proteins, bacterial cells that express the modified proteins, and cell free synthesis systems containing modified RF1. The disclosure further provides methods for reducing the deleterious activity of a modified protein in a cell free synthesis system by contacting the modified protein with OmpT1. Also provided are methods for reducing RF1 competition at an amber codon in the cell free synthesis system, and methods for expressing a protein in the cell free synthesis system. The modified proteins of the invention can be used to increase the yield of proteins having non-natural amino acids incorporated at an amber codon.

Abstract: The present invention relates to alpha-amylase variants having an improved stability as compared to the parent alpha-amylase. The invention further relates to use of the variants, compositions comprising the variants, and methods of producing the variants.

Abstract: The invention relates to an endocellulase catalytic domain comprising the sequence of SEQ ID NO: 1 or a functionally equivalent variant of said catalytic domain that substantially maintains or improves its catalytic activity. The invention also relates to a polypeptide, a nucleic acid, an expression cassette, a vector or a host cell. Additionally, the invention relates to the use of an endocellulase catalytic domain or the polypeptide of the invention for hydrolysing cellulose, producing bioethanol or as a detergent. The invention also relates to a method for hydrolysing cellulose and for producing bioethanol.

Abstract: Disclosed are isolated polypeptides having protease activity, and polynucleotides encoding the polypeptides. Nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides are also disclosed.

Abstract: A horseshoe crab Factor C protein having activity of Factor C, wherein the horseshoe crab is selected from Tachypleus tridentatus, Limulus polyphemus, and Carcinoscorpius rotundicauda, and wherein the horseshoe crab Factor C protein is produced through being recombinantly expressed from a Chinese Hamster Ovary (CHO) DG44 cell or HEK cell.

Abstract: The present invention relates a variant polypeptide having geranylgeranyl pyrophosphate synthase activity, which variant polypeptide comprises an amino acid sequence which, when aligned with a geranylgeranyl pyrophosphate synthase comprising the sequence set out in SEQ ID NO: 1, comprises at least one substitution of an amino acid residue corresponding to any of amino acids at positions 92, 100 or 235 said positions being defined with reference to SEQ ID NO: 1 and wherein the variant has one or more modified properties as compared with a reference polypeptide having geranylgeranyl pyrophosphate synthase activity. A variant polypeptide of the invention may be used in a recombinant host for the production of steviol or a steviol glycoside.

Abstract: The present invention relates to isolated polypeptides having cellobiohydrolase activity and polynucleotides encoding the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides.

Abstract: The present invention relates to isolated polypeptides having cellobiohydrolase activity and isolated polynucleotides encoding the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides.

Abstract: The present disclosure is intended to reduce the amount of glycerin produced as a by-product in ethanol fermentation to a significant extent using a transgenic yeast comprising a gene having the pentose assimilating ability and encoding glycerin dehydrogenase having a mitochondrial transport signal introduced thereinto.

Abstract: The present invention relates to a recombinant microorganism having an enhanced ability to produce heme, coproporphyrin III (Copro III), and uroporphyrin III (Uro III), and a method for producing heme, coproporphyrin III, and uroporphyrin III using same. When using a recombinant microorganism incorporating a gene that codes glutamyl-tRNA reductase (HemA), glutamate-1-semialdehyde aminotransferase (HemL), and diphtheria toxin repressor (DtxR), which is a transcription factor capable of inducing the expression of genes related to heme metabolic pathways, porphyrin-based structures can be produced at high yield, and thus the method is economic.

Abstract: The present invention relates to the field of fermentation, more particularly to ethanol production. Even more particularly the present invention relates to reduced aroma production during fermentation processes. The present invention provides mutant alleles and chimeric genes useful to develop yeast strains to limit acetate ester levels during fermentation. In addition, the invention also relates to the use of such yeast strains as well as of compounds for the production of fermented foods and liquids with reduced acetate ester levels.

Abstract: The present invention provides a method for bioconversion of mogroside extracts into siamenoside I, comprising: using (1) DbExg1 protein or (2) a microorganism expressing the DbExg1 protein to contact or to cultivate with the mogroside extracts. The present invention can convert the mogroside extracts into siamenoside I, which has a higher sweetening power and better taste than other mogrosides. The method of the present invention uses a microorganism expressing the responsible enzyme, DbExg1, which was identified as a mediator of mogroside V conversion into siamenoside I in the present invention, so that siamenoside I was preferentially produced. Thus, the use of the method of the present invention provides a feasible approach to produce large quantities of the natural sweetener, siamenoside I, which can then be applied in several industries.

Abstract: Disclosed is an alcohol dehydrogenase mutant and application thereof in cofactor regeneration, and belongs to the technical fields of enzyme engineering and bioengineering. The alcohol dehydrogenase mutant is obtained by mutating valine at position 84 and/or tyrosine at position 127 in alcohol dehydrogenase having an original amino acid sequence as set forth in SEQ ID No. 1. The alcohol dehydrogenase mutant has high activity for a variety of alcohol co-substrates, and can catalyze these enzyme co-substrates for the regeneration of cofactor NADPH. Compared with the wild-type alcohol dehydrogenase KpADH, the alcohol dehydrogenase mutant has higher activity and catalytic efficiency, and for co-substrate 1,4-butanediol, its kcat value can be up to 75.9 min?1, its kcat/Km value can be up to 2009 min?1·M?1, and its Km value can be as low as 11.3 mM. Therefore, the alcohol dehydrogenase mutant has a higher value in industrial application.

Abstract: The present invention relates to the field of genetic engineering, particularly to phytase variant YeAPPA having improved pepsin resistance and acid resistance, and increased catalytic efficiency, by substituting Leucine at the 162th site of the sequence set forth in SEQ ID NO.1 with glycine or proline or substituting glutamic acid at the 230th site of the sequence set forth in SEQ ID NO.1 with glycine, proline or arginine, in the benefit of the development of economical feed enzyme industry.

Abstract: The invention provides an animal feed composition comprising microbial ?-amylase. The invention further provides methods of increasing the growth (weight gain), the average daily weight gain or the efficiency of feed utilization by an animal or reducing the number of days needed to achieve a desired weight in an animal, comprising feeding to the animal an animal feed composition of the present invention.

Abstract: According to the present invention, theanine can efficiently be produced without exogenously adding ethylamine and without accumulation or leftover of ethylamine as a byproduct, by using a microorganism having enhanced activity to produce ethylamine with acetaldehyde and alanine as substrates and having enhanced activity of ?-glutamylmethylamide synthetase or glutaminase.

Abstract: The invention provides microorganisms genetically modified to overexpress thermophilic lysine decarboxylase polypeptides in a mesophilic host to enhance the production of lysine and lysine derivatives by the microorganism, method of generating such microorganism, and methods of producing lysine and lysine derivatives using the genetically modified microorganisms.