C12N1/21

Antibodies against growth differentiation factor 15 and uses thereof

Provided herein are monoclonal antibodies (e.g., human antibodies) binding to human Growth Differentiation Factor 15 protein (hereinafter, sometimes referred to as “GDF15”), and pharmaceutical compositions and methods of treatment comprising the same.

Method for producing 3-hydroxy-4-aminobenzoic acid compound
11312980 · 2022-04-26 · ·

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.

Universal platform for genetic code expansion

Methods and compositions are described for selecting and identifying orthogonal aminoacyl synthetase-tRNA pairs and their use to incorporate unnatural amino acids in a site-specific manner in proteins. Specifically described is a novel E. coli tryptophanyl synthetase-tRNA pair that functions as both an opal and amber suppressor and that incorporates tryptophan analogs into proteins.

L-aspartate alpha-decarboxylase mutant and application thereof

The disclosure discloses an L-aspartate α-decarboxylase mutant and application thereof, and belongs to the technical field of enzyme engineering. In the disclosure, lysine at position 221 of L-aspartate α-decarboxylase is mutated to arginine, glycine at position 369 is mutated to alanine, and the obtained new mutant enzymes have better temperature tolerance and are beneficial to industrial production. The K221R and G369A recombinant strains are subjected to high-density fermentation, and with sodium L-aspartate as a substrate, a whole cell catalytic reaction is carried out to prepare β-alanine. Compared with a chemical production method, the method has the advantages that the production process is safe and clean, and has no environmental pollution. Compared with a pure enzyme catalysis method, the method has the advantages that the operation is simple and convenient. The yield of the final product β-alanine reaches 91% and 90% respectively, and the concentration reaches 162.15 g/L and 160.42 g/L respectively.

Phytase mutant

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.

Machine learning gene mining method and phosphinothricin dehydrogenase mutant for amino translocation

Disclosed are a machine learning gene mining method and a phosphinothricin dehydrogenase mutant for amino translocation. The phosphinothricin dehydrogenase mutant for amino translocation is obtained by mutation of a wild-type phosphinothricin dehydrogenase with an amino acid sequence as shown in SEQ ID No.2 at one of the following sites: (1) E263D-K134R-H96A-R290V; (2) E263D-K134R-H96A; (3) E263D-K134R; (4) E263D; (5) E263N; (6) E263C; and (7) E263G. The present invention utilizes the site-saturation mutagenesis technology to mutate a phosphinothricin dehydrogenase gene as shown in SEQ ID No. 1, finds that the 263rd, 134th, 290th and 290th positions are the key sites affecting enzyme activity and stereoselectivity, and obtains a mutant with enzyme activity and ee value much higher than those of the parent phosphinothricin dehydrogenase.

Compositions comprising polypeptides having xylanase activity and polypeptides having arabinofuranosidase activity

The present invention relates to compositions comprising polypeptides having xylanase activity and polypeptides having arabinofuranosidase activity for use in, e.g., animal feed. The present invention further relates to polypeptides having arabinofuranosidase activity, polypeptides having xylanase 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.

Fluorescence-based reporters for mutagenesis detection in <i>E. coli </i>

Direct detection of mutagenesis in prokaryotes by reversion of an inactivating mutation (reversion mutation assay), producing a quantitative signal for in vivo mutagenesis, may greatly reduce the amount of test chemicals and labor involved in these assays. Further, transcriptional coupling of β-lactamase reversion and GFP, translational fusion between β-lactamase and GFP with stop codon in GFP, and a novel dual reporter to monitor continuous mutagenesis may be used in methods described herein.

Producing 3-hydroxycarboxylic acid and ketone using polyketide synthases

The present invention provides for a polyketide synthase (PKS) capable of synthesizing a 3-hydroxycarboxylic acid or ketone. The present invention also provides for a host cell comprising the PKS and when cultured produces the 3-hydroxycarboxylic acid or ketone.

Metabolic engineering for simultaneous consumption of Xylose and glucose for production of chemicals from second generation sugars

The present disclosure provides methods for genetically modifying microbes to produce a microbe capable of simultaneous consumption of xylose and glucose to increase the productivity output of desired chemical products. The disclosure further provides modified bacteria that are capable of simultaneous consumption of xylose and glucose, and compositions comprising the microbes.