Abstract: The invention provides methods for producing soluble di-chain BoNT/A protein.

Abstract: Methods and compositions related to the use of a protein with kynureninase activity are described. For example, in certain aspects there may be disclosed a modified kynureninase capable of degrading kynurenine. Furthermore, certain aspects of the invention provide compositions and methods for the treatment of cancer with kynurenine depletion using the disclosed proteins or nucleic acids.

Abstract: The present disclosure relates to proteases having an amino acid sequence with at least 70% sequence identity to the amino acid sequence given in SEQ ID No. 1, across its whole length, and comprising an amino acid substitution on at least one of the positions P9, Q10, Q62, L82, P86, N130, T141, N187, S236 or T253, relating in each case to the numbering according to SEQ ID No. 1. The present disclosure also relates to the production and use thereof. Said type of proteases have a very good cleaning performance.

Abstract: The present invention relates to a novel polypeptide which displays IgG cysteine protease activity, and in vivo and ex vivo uses thereof. Uses of the polypeptide include methods for the prevention or treatment of diseases and conditions mediated by IgG, and methods for the analysis of IgG.

Abstract: Provided is a technology related to a horseshoe crab factor B variant, and also provided is means for performing endotoxin measurement with high sensitivity. A polypeptide having an amino acid sequence in which the amino acid residue at the 193-position in an amino acid sequence of a polypeptide of horseshoe crab factor B is substituted with a cysteine (Cys) residue, is produced. Endotoxin measurement can be carried out with high sensitivity by configuring a Limulus reagent by combining this polypeptide with horseshoe crab factor C.

Abstract: A truncated and modified Serratiopeptidase or a variant thereof, and polynucleotides encoding the same. The truncated and modified Serratiopeptidase may have an amino acid sequence including amino acids 1 to 344, and amino acids 1 to 380 of SEQ ID NO: 1. The truncated and modified Serratiopeptidase may further include a first Cysteine (C) residue at a N-terminus of the truncated and modified Serratiopeptidase, substituted for at least one of Alanine 8 and Leucine 12 of SEQ ID NO: 1; and a second Cysteine residue at a C-terminus of the truncated and modified Serratiopeptidase, substituted for at least one of Valine 339 and Arginine 302 of SEQ ID NO: 1. The first and the second Cysteine residues may be adapted to form at least one disulfide bond including at least one of C8-C339, and C12-C302 disulfide bonds between the N-terminus and the C-terminus of the truncated and modified Serratiopeptidase.

Abstract: Provided in this disclosure are chimeric peptides that include a spacer domain, the spacer domain itself, substrates (e.g., implants) coated with the chimeric peptides, and methods for making and using the coated substrates.

Abstract: A phosphate-free automatic dishwashing cleaning composition comprising a protease wherein the protease has at least 80%, preferably at least 85%, more preferably at least 90% and especially at least 96% identity with the amino acid sequence of SEQ ID NO:1 or with the amino acid sequence of SEQ ID NO:2 and wherein the protease comprises amino acid substitutions selected from the group consisting of: (i) at least two amino acid substitutions selected from the group consisting of: X198G/A/K/L/Q/R/T/V/S/L, X207Q, X211Q/N and X212Q in combination with at least three amino acid substitutions selected from the group consisting of: X039E, X074D, X099R, X126A, X127E and X128G; or (ii) X039E-X074D-X099R-X116R-X126A-X127E-X128G-X211Q; X039E-X074D-X099R-X126A-X127E-X128G-X211N; X039E-X074D-X099R-X126A-X127E-X128G-X211Q; X039E-X074D-X099R-X126A-X127E-X128G-X207Q; or (iii) any of the proteases of (i) and (ii) further comprising at least one amino acid substitution selected from X242D and X256E; or (iv) X039E-X074D-X099R

Abstract: The present disclosure relates to a novel polypeptide having an ability to export an ornithine-based product, and a method for producing an ornithine-based product using the same.

Abstract: The present invention relates to isolated polypeptides having protease activity, animal feed additives comprising said polypeptides improving the nutritional value of an animal feed by adding the protease, invention also relates to polynucleotides encoding the polypeptides, nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing the polypeptides.

Abstract: The present disclosure provides AprL-clade protease enzymes, including variant AprL-clade protease enzymes, nucleic acids encoding same, and compositions and methods related to the production and use thereof, including an AprL-clade variant subtilisin enzyme that has improved stability and/or soil removal compared to a parent AprL-clade subtilisin enzyme.

Abstract: Described are compositions, in particular lyophilizates, containing proteolytic enzymes, and methods for producing the compositions. Typically these compositions contain one or more proteases with collagenase activity and a neutral protease, for example, thermolysin. The compositions are free of acetate salts. Surprisingly, such compositions can be dissolved in water more rapidly than lyophilized protease mixtures of the state of the art.

Abstract: The present invention provides serine protease variants produced there from. Specifically, the present invention provides serine protease variants having one or more substitutions as compared to a reference serine protease. In addition, the present invention provides compositions comprising these serine protease variants. In some embodiments, the present invention provides cleaning compositions comprising at least one of these serine protease variants.

Abstract: The present invention relates to protease variants, having improved properties compared to the parent protease, in particular variants of a serine protease belonging to family 53 derived from a strain of Meripilus giganteus. The variants according to the invention have in particular increased thermo-stability, e.g., increased residual activity after 30 min at a temperature in the range from 55 to 60° C. and/or increased thermal denaturation temperature, compared to the parent Meripilus giganteus protease. 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 invention is a novel reporter system for measuring protein-protein interactions. The system uses a pair of functionalized coiled coil subunits that spontaneously form two separate homo-oligomers when expressed in cells. The coiled coil subunits are functionalized with fluorescent proteins and complementary interacting proteins. Upon an activation stimulus which promotes the protein-protein interaction, the interacting proteins drive the formation of multivalent aggregates of the homo-oligomers in phase-shifted droplets. The highly concentrated fluorescent proteins in these structures provide high brightness over background fluorescence and a readily observed, quantitative and dynamic indicator of the protein-protein interaction. The reporters and assay methods are amenable to cells and whole organisms.

Abstract: The present invention relates to mutants of a parent Trichoderma strain, comprising a polynucleotide encoding a polypeptide and one or more (several) genes selected from the group consisting of a first subtilisin-like serine protease gene, a first aspartic protease gene, a trypsin-like serine protease gene, a second subtilisin-like serine protease gene, and a second aspartic protease gene, wherein the one or more (several) genes are modified rendering the mutant strain deficient in the production of one or more (several) enzymes selected from the group consisting of a first subtilisin-like serine protease, a first aspartic protease, a trypsin-like serine protease, a second subtilisin-like serine protease, and a second aspartic protease, respectively, compared to the parent Trichoderma strain when cultivated under identical conditions. The present invention also relates to methods of producing a polypeptide in such mutants and methods for producing such mutants.

Abstract: Provided herein is a thermolabile proteinase and methods of using the same. In some embodiments, the thermolabile proteinase may comprise an amino acid sequence that is at least 90% identical to any of SEQ ID NOs:1-11 and at least one amino acid substitution in helix 3. The thermolabile proteinase is active at a temperature in the range of 4° C.-40° C. and is inactivated by raising the temperature to above 50° C., where the proteinase is substantially inactive at 65° C.

Abstract: Disclosed is a modified microorganism producing putrescine or ornithine, and a method for producing putrescine or ornithine using the same.

Abstract: A thermolysin solution has further improved stability as a result of the thermolysin solution containing thermolysin at a concentration that is 0.1 mg/mL or higher and the thermolysin solution having a pH that is adjusted to higher than 9.0. The thermolysin solution preferably has a pH in the range of 9.5-11.5.

Abstract: A DNA sequence encoding Der p1 protein having a particular base sequence is codon-optimized for the Pichia pastoris expression system, which is conducive to expressing Der p1 in Pichia pastoris. After gene optimization and adding an activating element to increase the expression of Der p1 in molecular level, it was found that Der p1 is expressed at a higher level as compared with the prior art and has biological activity similar to the natural protein.