Abstract: Polypeptides having phytase activity and polynucleotide sequences encoding the phytases are provided. The gene expresses the phytase at a level of at least 7 g/L to 40 g/L. The phytase have higher specific activity, retain activity at low pH, and retain activity at high temperature. The phytase can be used in a variety of compositions including food, feed, pharmaceuticals, and cleaning.

Abstract: The present invention provides engineered human alpha-galactosidase polypeptides and compositions thereof. The engineered human alpha-galactosidase polypeptides have been optimized to provide improved stability under both acidic (pH<4.5) and basic (pH>7) conditions. The invention also relates to the use of the compositions comprising the engineered human alpha-galactosidase polypeptides for therapeutic purposes.

Abstract: The present invention relates to the technical field of protein engineering, and, in particular, to a xylanase mutant with improved heat tolerance. The present invention artificially introduces two or three unnatural disulfide bridges into xylanase by site-directed mutagenesis and obtains the mutants XynA1 and XynA2 with improved heat tolerance, especially the mutant XynA2 into which three disulfide bridges are introduced, achieving residual enzyme activity of 75% after treatment at 80° C. for 5 min, 72% higher than the residual enzyme activity of the mutant XynA1. The present invention further obtains, by screening, three mutation sites Q51N, H143K, and Q161F that can significantly increase the heat tolerance of mutants, and introduction of the mutation sites into the XynA1 and XynA2 xylanases, whether at a single point or a combination of two points or a combination of three points, can effectively improve the heat tolerance of the mutants.

Abstract: Described herein is a variant pol6 polymerase having at least one mutation selected from H223, N224, Y225, H227, I295, Y342, T343, I357, S360, L361, I363, S365, S366, Y367, P368, D417, E475, Y476, F478, K518, H527, T529, M531, N535, G539, P542, N545, Q546, A547, L549, I550, N552, G553, F558, A596, G603, A610, V615, Y622, C623, D624, I628, Y629, R632, N635, M641, A643, I644, T647, I648, T651, I652, K655, W656, D657, V658, H660, F662, L690 and combinations thereof.

Abstract: Described herein is a variant pol6 polymerase having at least one mutation selected from H223, N224, Y225, H227, I295, Y342, T343, I357, S360, L361, I363, S365Q, S366, Y367, P368, D417, E475, Y476, F478, K518, H527, T529, M531, N535, G539, P542, N545, Q546, A547, L549, I550, N552, G553, F558, A596, G603, A610, V615, Y622, C623, D624, I628, Y629, R632, N635, M641, A643, I644, T647, I648, T651, I652, K655, W656, D657, V658, H660, F662, L690 and combinations thereof.

Abstract: The invention relates to processes of producing a fermentation product, comprising liquefying a starch containing material with an alpha-amylase; pre-saccharifying and/or saccharifying and fermenting using a fermentation organism in the presence of a carbohydrate source generating enzyme and a cellulolytic composition The invention also relates to methods of dewatering whole stillage.

Abstract: The invention relates to novel 7ß-hydroxysteroid dehydrogenase mutants, to the sequences which encode these enzyme mutants, to processes for the preparation of the enzyme mutants and to their use in enzymatic reactions of cholic acid compounds, in particular in the preparation of ursodeoxycholic acid (UDCS). The invention also relates to novel processes for the synthesis of UDCS using the enzyme mutants; and to the preparation of UDCS using recombinant, multiply-modified microorganisms.

Abstract: The present disclosure relates to the co-expression of an endonuclease with an end-processing enzyme for the purpose of enhanced processing of the polynucleotide ends generated by endonuclease cleavage.

Abstract: A biotechnological production of tryptophan and derivatives thereof, as well as a method for an enhanced microbial L-tryptophan synthesis. In one aspect the invention provides a bacterial cell being genetically modified to express anindole-3-glycerol phosphate synthase, IGPs, the IGPs being less sensitive to inhibition or even being activated by anthranilate compared to the wild type IGPs of the bacterial cell.

Abstract: Engineered Cas9 systems are disclosed herein. For example, Cas9-marker fusion proteins are provided. Peptide linkers which facilitate fusion of heterologous proteins to CRISPR proteins in ways that preserve CRISPR functionality are also provided.

Abstract: A novel protein deamidase having an activity of directly acting on a side chain amide group of an asparagine residue in a protein to form a side chain carboxyl group and release ammonia, a microorganism that produces the same, a gene encoding the same, a method for producing the same, and use of the same are provided. A bacterium classified into the class Actinobacteria is cultured to generate protein deamidase, and the enzyme is collected from culture.

Abstract: A modified endoinulinase is provided, comprising modified wild-type T. purpuregenus endoinulinase, or a functional fragment thereof, in which an amino acid residue at each one of one or more positions corresponding to 128, 316, 344, 350 or 504 of wild-type T. purpuregenus endoinulinase is substituted, wherein: (i) a tyrosine residue corresponding to Y128 is substituted with H, K or R; a glutamate residue corresponding to E344 is substituted with K, H or R; and a threonine residue corresponding to T504 is substituted with M, S or Y; and optionally an alanine residue corresponding to A316 is substituted with T, S, C or M; (ii) a tyrosine residue corresponding to Y128 is substituted with H, K or R; a glutamate residue corresponding to E344 is substituted with K, H or R; a threonine residue corresponding to T504 is substituted with M, S or Y; and a glutamine residue corresponding to Q350 is substituted with L, G, A, V or I; or (iii) a tyrosine residue corresponding to Y128 is substituted with H, K or R.

Abstract: The invention provides fabrics that incorporate enzymes that inactivate microbial pathogens, particularly enveloped viral particles such as those of Influenza virus and Coronavirus such as Covid-19. The fabrics of the invention may be used in the production of various items including protective facemasks.

Abstract: This invention relates to the production of succinic acid and other chemicals derived from phosphoenolpyruvate (PEP) by fermentation with a microorganism in which the fermentation medium contains one or more sugars, and in which one or more of the sugars is imported into the cell by facilitated diffusion. As a specific example, succinic acid is produced from a glucose-containing renewable feedstock through fermentation using a biocatalyst. Examples of such a biocatalyst include microorganisms that have been enhanced in their ability to utilize glucose as a carbon and energy source. The biocatalysts of the present invention are derived from the genetic manipulation of parental strains that were originally constructed with the goal to produce one or more chemicals (for example succinic acid and/or a salt of succinic acid) at a commercial scale using feedstocks that include, for example, glucose, fructose, or sucrose.

Abstract: The present disclosure provides improved genome editing compositions and methods for editing a CBLB gene. The disclosure further provides genome edited cells for the prevention, treatment, or amelioration of at least one symptom of, a cancer, an infectious disease, an autoimmune disease, an inflammatory disease, or an immunodeficiency.

Abstract: Provided herein are systems and methods for characterizing target/ligand engagement. In particular, luciferase-labeled polypeptide targets are used to detect or quantify target/ligand engagement (e.g., within a cell or cell lysate).

Abstract: The present disclosure describes a variant polypeptide having lipolytic activity, wherein the variant has an amino acid sequence which, when aligned with the amino acid sequence as set out in SEQ ID NO: 2, comprises at least one substitution of an amino acid residue at a position corresponding to any of the positions 53, 112, 141, 178, 179, 182, 202, 203, 235, 282, 284, said positions being defined with reference to SEQ ID NO: 2, and wherein said variant has at least 70% identity with the mature polypeptide having lipolytic activity as set out in SEQ ID NO: 2. Such a variant polypeptide may be used in the preparation of a baked product.

Abstract: Disclosed is an engineered thermolabile mutant of Serratia Marcescens Nuclease. In the same buffer as used for optimal enzyme activity, after 60° C. for 20 min, while the wild type retained 12.5% activity, the thermolabile mutant R146D/D156R/D229R/D245R (SEQ ID NO: 12, without the first 21 amino acids, which are a signal peptide) retained only 0.39% activity. Heat inactivation of the mutant, when it is used for protein purification, can be used after a period when substantial DNA in a protein has been degraded, but before unwanted degradation takes place.

Abstract: Methods of modulating the properties of a cell culture expressing a protein of interest are provided. In various embodiments the methods relate to the overexpression of proteins involved in the N-glycosylation pathway.

Abstract: The disclosure provides a modified UDP-GlcNAc:Lysosomal Enzyme GlcNAc-1-phosphotransferase with enhanced ability to phosphorylate lysosomal enzymes and methods of use thereof.