Abstract: The present disclosure provides recombinant microorganisms and methods for the production of 4-HMF, 2,4-furandimethanol, furan-2,4-dicarbaldehyde, 4-(hydroxymethyl)furoic acid, 2-formylfuran-4-carboxylate, 4-formylfuran-2-carboxylate, and/or 2,4-FDCA from a carbon source. The method provides for engineered microorganisms that express endogenous and/or exogenous nucleic acid molecules that catalyze the conversion of a carbon source into 4-HMF, 2,4-furandimethanol, furan-2,4-dicarbaldehyde, 4-(hydroxymethyl)furoic acid, 2-formylfuran-4-carboxylate, 4-formylfuran-2-carboxylate, and/or 2,4-FDCA. The disclosure further provides methods of producing polymers derived from 4-HMF, 2,4-furandimethanol, furan-2,4-dicarbaldehyde, 4-(hydroxymethyl)furoic acid, 2-formylfuran-4-carboxylate, 4-formylfuran-2-carboxylate, and/or 2,4-FDCA.

Abstract: Provided is a method for manufacturing a 3-hydroxy-4-aminobenzoic acid by using a microorganism. The method for manufacturing a 3-hydroxy-4-aminobenzoic acid comprises a step of bringing a 4-aminobenzoic acid into contact with a microorganism that produces the following polypeptide (A) or (B): (A) a polypeptide consisting of an amino acid sequence shown in SEQ ID NO: 2 or a polypeptide consisting of an amino acid sequence that has at least 90% identity to the amino acid sequence shown in SEQ ID NO: 2 and has 4-hydroxybenzoate hydroxylase activity, (B) a polypeptide consisting of an amino acid sequence shown in SEQ ID NO: 6 or a polypeptide consisting of an amino acid sequence that has at least 90% identity to the amino acid sequence shown in SEQ ID NO: 6 and has 4-hydroxybenzoate hydroxylase activity.

Abstract: Provided are a hexuronate C4-epimerase variant with improved activity in converting D-fructose by D-tagatose of hexuronate C4-epimerase and a method for production of D-tagatose using them.

Abstract: The invention provides a non-naturally occurring microbial organism having an adipate, 6-aminocaproic acid or caprolactam pathway. The microbial organism contains at least one exogenous nucleic acid encoding an enzyme in the respective adipate, 6-aminocaproic acid or caprolactam pathway. The invention additionally provides a method for producing adipate, 6-aminocaproic acid or caprolactam. The method can include culturing an adipate, 6-aminocaproic acid or caprolactam producing microbial organism, where the microbial organism expresses at least one exogenous nucleic acid encoding an adipate, 6-aminocaproic acid or caprolactam pathway enzyme in a sufficient amount to produce the respective product, under conditions and for a sufficient period of time to produce adipate, 6-aminocaproic acid or caprolactam.

Abstract: The invention relates to a polypeptide comprising an exoglucanase catalytic domain comprising a sequence selected from the group consisting of SEQ ID NO: 1, SEQ ID NO: 2 and SEQ ID NO: 3, and to a polypeptide having beta-glucosidase activity comprising a sequence selected from the group consisting of SEQ ID NO: 6, SEQ ID NO: 7 and SEQ ID NO: 8, and to functionally equivalent variants thereof that maintain or improve their catalytic activity. Additionally, the invention relates to an enzyme cocktail comprising said polypeptide(s) and an endoglucanase.

Abstract: Provided are a novel 3-hydroxypropionate-lactate block copolymer [P(3HP-b-LA)], and a method for preparing same, comprising: a) transforming a recombinant microorganism modified to be incapable of biosynthesizing lactic acid with a vector including a 3-hydroxypropionyl-CoA biosynthesis gene and a polyhydroxyalkanoate (PHA) synthetase gene, and a vector including a lactate biosynthesis gene and a gene of an enzyme that converts lactate to lactyl-CoA; (b) synthesizing poly(3-hydroxypropionate) (P(3HP)) by culturing the recombinant microorganism using a glycerol as a carbon source; and (c) inhibiting P(3HP) production by adding IPTG and glucose, and biosynthesizing polylactate (PLA) at the end of P(3HP) synthesized in step (b) by enabling the expression of a lactate biosynthesis enzyme and an enzyme that converts lactate to lactyl-CoA. Also provided is a recombinant microorganism produced in step a).

Abstract: Provided herein are inhibitor-resistant luciferase mutants, and methods of use thereof. In particular, luciferase mutants are provided that are thermal stable and exhibit improved stability in the presence of luciferin break-down products, such as dehydroluciferin. Further provided are assay systems comprising inhibitor-resistant luciferase mutants and amino acid sequences of the inhibitor-resistant luciferase mutants.

Abstract: The invention relates to recombinant microorganisms and methods for producing mogroside compounds and mogroside precursors.

Abstract: Bacterial strain Clostridium histolyticum was deposited in CCM (Czech Collection of Microorganisms at Masaryk University, Faculty of Science) under No. CCM 8656. This strain produces proteolytic enzymes including collagenase, elastinase, neutral proteases and clostripain under anaerobic conditions at a temperature from 25° C. to 45° C. The strain is used for the production of a mixture of two collagenases, col 1 and col 2, with molecular weight 116 kDa and 126 kDa, and possibly clostripain. The mixture of the above-mentioned collagenases and possibly clostripain obtained from the above-mentioned strain is used for the isolation of Langerhans islets.

Abstract: The present invention relates to pharmaceuticals and modified beta-lactamases. Specifically, the invention relates to novel recombinant beta-lactamases and pharmaceutical compositions comprising the beta-lactamases. Also, the present invention relates to methods for modifying a beta-lactamase, producing the beta-lactamase and treating or preventing beta-lactam antibiotic induced adverse effects. Furthermore, the present invention relates to the beta-lactamase for use as a medicament and to the use of the beta-lactamase in the manufacture of a medicament for treating or preventing beta-lactam antibiotics induced adverse effects. Still further, the invention relates to a polynucleotide and a host cell comprising the polynucleotide.

Abstract: The present invention concerns a detergent and a pharmaceutical composition comprising a deoxyribonuclease (DNase), wherein the DNase is obtained from a fungal source. It further concerns a laundering method and the use of DNase. The present invention further relates to polypeptides having DNase activity, nucleotides encoding the polypeptide, as well as methods of producing the polypeptides.

Abstract: Provided are phytase mutants, preparation methods therefor and uses thereof, DNA molecule encoding each of the phytase mutants, a vector comprising the DNA molecule, and a host cell comprising the vector.

Abstract: The disclosure relates to a sucrose phosphorylase mutant with improved enzyme activity, and construction method thereof and use thereof, and belongs to the technical field of genetic engineering. The amino acid sequence of the mutant of the disclosure is as shown in SEQ ID NO: 1. The mutant of the disclosure is based on sucrose phosphorylase derived from Leuconostoc mesenteroides, and subjected to site-directed mutagenesis to improve the enzyme activity of sucrose phosphorylase. The mutant is expressed in Corynebacterium glutamicum and used as a whole cell catalyst to produce 2-O-?-D-glycerol glucoside. At a 5 L fermentation tank level, a large quantity of 2-O-?-D-glycerol glucoside can be produced efficiently in a short time, which is conducive to expanding the prospect of industrial application of sucrose phosphorylase for the production of 2-O-?-D-glycerol glucoside and realizing its large-scale industrial application.

Abstract: The present invention relates to protease variants and methods for obtaining protease variants. The present invention also relates to polynucleotides encoding the variants; nucleic acid constructs, vectors, and host cells comprising the polynucleotides; and methods of using the variants.

Abstract: The disclosure relates to acetyl-CoA carboxylase (ACC) variants and host cells expressing them for the production of malonyl-CoA derived compounds including fatty acid derivatives. Further contemplated are methods of producing increased amounts of malonyl-CoA derived compounds and related cell cultures.

Abstract: The present disclosure relates to a novel chitinolytic enzyme, particularly to a chitinolytic enzyme including an exo-?-N-acetylglucosaminidase (Clocel_3193) constituting a cellulosome derived from Clostridium cellulovorans as an active ingredient. The present disclosure allows utilization of chitin biomass which has not been used formerly as a raw material and allows environment-friendly production of N-acetylglucosamine. In addition, since the Clocel_3193 has a cell wall binding ability and degrading ability, the Clocel_3193 may be used in an antifungal composition.

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

Abstract: The present disclosure relates to Cas9 nuclease variants and methods of producing and using such variants.

Abstract: The present invention relates to alpha-amylase variants with improved stability in the presence of glucose and/or relatively higher activity on long chain versus short chain substrates. The present encoding invention also relates to polynucleotides encoding the variants; nucleic acid constructs, vectors, and host cells comprising the polynucleotides; and methods of using the variants.

Abstract: Disclosed are recombinant strain of a genus Corynebacterium capable of producing biliverdin IX-alpha (IX?) and a method of producing biliverdin IX-alpha using the same. The recombinant strain is capable of synthesizing biliverdin IX-alpha in an environmentally friendly manner using only glucose without the addition of any nitrogen source, thus replacing the synthesis of biliverdin IX-alpha through chemical treatment, which is a conventional synthetic method causing environmental pollution problems.