Abstract: The present invention relates to alpha-amylase 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: There is provided chimeric polypeptides capable of converting xylose to xylulose, engineered host cells that express the chimeric polypeptides, methods of creating chimeric polypeptides, and methods of fermenting cellulosic biomass to produce biofuels, including ethanol.

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, 1644, T647, I648, T651, I652, K655, W656, D657, V658, H660, F662, L690 and combinations thereof.

Abstract: Provided herein are processes and microorganisms which utilize both protein hydrolysates and carbohydrates from biomass feedstocks to produce renewable hydrocarbon compositions. Advantages of the disclosed methods may be recognized in fuel blends comprising such hydrocarbon compositions.

Abstract: Cleaning compositions having an enzyme system, where the enzyme system includes a nuclease enzyme, an extracellular-polymer-degrading enzyme, and a cleaning adjunct. Methods of making and using such cleaning compositions. Use of an extracellular-polymer-degrading enzyme.

Abstract: An acyl-ACP thioesterase consisting of an amino acid sequence of the 115th to 274th amino acids set forth in SEQ ID NO: 1; an acyl-ACP thioesterase gene encoding the protein; a transformant having the gene; and a method of producing a lipid using the transformant.

Abstract: Provided herein in some embodiments is a non-naturally occurring variant of a wild type restriction enzyme defined by SEQ ID NO: 20, wherein the variant has at least a 2 fold increase in cleavage at 5-? glucosylhydroxymethylcytosine (5?ghmC) compared with methylcytosine relative to the wild type enzyme. Methods for examining hydroxymethylation of a DNA sample using the variant enzyme are also provided.

Abstract: Provided is a microorganism having high sophorolipid production capability. Disclosed is a sophorolipid-producing yeast mutant strain, in which a polypeptide consisting of the amino acid sequence set forth in SEQ ID NO:2 or an amino acid sequence having at least 90% identity therewith, has been deleted or deactivated.

Abstract: Reaction solutions are disclosed herein comprising water, sucrose and a glucosyltransferase enzyme that synthesizes poly alpha-1,3-glucan. The glucosyltransferase enzyme can synthesize insoluble glucan polymer having at least 50% alpha-1,3 glycosidic linkages and a number average degree of polymerization of at least 100. Further disclosed are methods of using such glucosyltransferase enzymes to produce insoluble poly alpha-1,3-glucan.

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 invention relates to variant thioesterases and their use in plants, e.g., to increase enzymatic activity and to promote increased production of mid-chain length fatty acids (e.g., 8 to 14 carbons) and at desired ratios. Further disclosed herein are methods of manufacturing renewable chemicals through the manufacture of novel triglyceride oils followed by chemical modification of the oils. Oils containing fatty acid chain lengths of C8, C10, C12 or C14 are also disclosed and are useful as feedstocks in the methods described herein.

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 disclosure relates to compositions and methods useful for the production of heterologous proteins in filamentous fungal cells.

Abstract: Clostridium perfringens can cause food poisoning and is a major agent in necrotic enteritis. As laws banning the use of antibiotics in animal feed become more common, the need for alternatives to antibiotics becomes greater. Peptidoglycan hydrolases that target the cell wall of specific bacteria are one such alternative. Genes for four endolysins, PlyCP10, PlyCP18, PlyCP33, and PlyCP41, were found within clusters of phage associated genes, likely prophages from strains Cp10, Cp18, Cp33, and Cp41. PlyCP18 and PlyCP33 harbor L-alanine amidase catalytic domains, and PlyCP10 and PlyCP41 have glycosyl hydrolase catalytic domains as predicted by BlastP and PFAM searches. All four genes were synthesized with E. coli codon optimization, expressed in E. coli expression vectors with a 6×His tag for nickel column purification, and the recombinant proteins purified. The four endolysins were capable of lysing the 66 C. perfringens strains tested but not the other bacteria tested.

Abstract: Disclosed herein are methods of making multifunctional microbial cellulases. The engineered multifunctional microbial cellulases disclosed herein exhibit improved activity over native cellulases.

Abstract: The invention comprises isolated, mutant, non-wild-type organophosphorus acid anhydrolase (OPAA) enzymes having two site mutations, methods of production, and methods of use to effectively degrade cylcosarin (GF) (cyclohexyl methylphosphonofluoridate) with greater catalytic efficiency than the wild-type OPAA.

Abstract: The invention relates to establishment of a series of artificial luciferases based on artificial amino acid sequences extracted by amino acid alignment of copepod-derived luciferase sequences in a database based on amino acid similarity. The invention provides high luminescence intensity, high luminescence stability, and a spectrum with increased wavelength as luminescence characteristics. A series of artificial luciferases (ALuc) was established. The group of ALucs has superior luminescence characteristics, such as an increase in luminescence intensity, an increase in luminescence stability, or an increase in wavelength of the luminescence spectrum, which were not obtained before. Further, by using the artificial luciferases (ALuc) of the invention, it is possible to provide a novel, superior bioassay system, such as a bioluminescent probe, two-hybrid assay, a luminescent capsule, or the like having improved measurement function.

Abstract: A recombinant protein and a preparation method and application thereof are provided. The recombinant protein includes a peptide, and the peptide includes an amino acid sequence after substitution of the sequence of SEQ ID NO: 1. The substitution includes at least one selected from the group consisting of the following substitutions: the amino acid at position 182 of SEQ ID NO: 1 is substituted with aspartic acid (Asp); the amino acid at position 268 of SEQ ID NO: 1 is substituted with aspartic acid (Asp); and the amino acid at position 384 of SEQ ID NO: 1 is substituted with tyrosine (Tyr). The recombinant protein is suitable for detecting glycated hemoglobin.

Abstract: The present invention relates to processes for producing fermentation products from starch-containing material, wherein an alpha-amylase and optionally a thermostable protease, pullulanase and/or glucoamylase are present and/or added during liquefaction, wherein a cellulolytic composition is present and/or added during fermentation or simultaneous saccharification and fermentation. The invention also relates to a composition suitable for use in a process of the invention.

Abstract: Described herein is a variant pol6 polymerase having at least one mutation selected from H223, N224, Y225, H227, 1295, 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.