20 results about "Enzyme variant" patented technology

The present invention relates to a method for obtaining a detergent composition comprising introducing (a) a variant of a parent lipase having at least 60% sequence identity with SEQ ID NO:2, having a substitution at a position D254 of the mature polypeptide corresponding to SEQ ID NO:2, and having lipase activity; and (b) an anionic surfactant, wherein the composition has increased stability compared to a corresponding composition containing the parent lipase.

The present disclosure relates, according to some embodiments, to systems, apparatus, compositions, methods, and workflows that include salt active nucleases (e.g., salt active nuclease variants) with desirable properties including, for example, salt tolerance.

A polypeptide comprising: a) milk-clotting enzyme activity, wherein the C / P ratio of clotting activity (C) to proteolytic activity (P) is equal to or greater than the C / P ratio of a polypeptide having the amino acid sequence of SEQ ID NO: 2; and b) alpha-S1-I casein fragment generating activity that is equal to or greater than the alpha-S1-I casein fragment generating activity of a polypeptide having the amino acid sequence of SEQ ID NO: 2; and / or c) a clotting time at pH 6.1 that is equal to or less than the clotting time of a polypeptide having the amino acid sequence of SEQ ID NO: 2.

A polypeptide having an amino acid sequence that, when compared with the amino acid sequence shown in SEQ ID NO:1, contains at least substitutions of amino acid residues corresponding to amino acids at sites 50, 51, 126, 135, and 221, wherein the sites are defined with reference to SEQ ID NO:1.

A sortase variant with improved catalytic activity and stability, in particular said mutant further comprises the mutations M155V / L200F or M155V / K162P, according to SEQ ID NO: 1, with respect to the parent sortase (SEQ ID NO: 2). Also the use of said sortase mutant is involved.

The present invention relates to a synthetic phytase which comprises (a) the amino acid sequence as set forth in SEQ ID NO. 1, (b) a variant of (a) having at least 70% sequence identity to SEQ ID NO. 1, or (c) a fragment, fraction or shuffled variant of (a) or (b) maintaining phytase activity, with the proviso that the phytase comprises one or more amino acid substitutions at one or more positions relative to SEQ ID NO. 1 selected from the group consisting of V13, T30, N37, K45, L46, T81, N83, A89, A113, Q121, Q122, A123, H128, K131, K139, A142, H143, Q162, S164, A166, S170, Q182, N184, G186, K187, L188, A194, M195, A200, I201, N202, D204, N206, K207, A209, S218, T219, L225, H228, K234, N239, E243, S248, Q256, F257, M260, S261, N270, P288, P292, A311, A314, L319, S320, W321, K344, K347, M355, L359, Q365, P367, E372, T388, Q404, and N405.

Disclosed are Type V CRISPR nucleases. Related Type V CRISPR nuclease ribonucleoprotein complexes, guide nucleic acids, recombinant expression vectors, kits, methods, and systems are also provided.

This application relates to the field of biotechnology and discloses a protein construct, a polynucleotide, and a recombinant host cell comprising a polypeptide having 1,3-α-glucanase activity. The polypeptide can be used in oral care products, including a polypeptide with the sequence shown in SEQ ID NO:3; and at least one oral care ingredient; wherein the polypeptide has activity in inhibiting and / or clearing biofilm formation of *Streptococcus mutans*. This application provides a polypeptide that inhibits the formation of *Streptococcus mutans* biofilm in the oral cavity, and an enzyme variant with biofilm-clearing effects, the enzyme variant providing stronger biofilm-clearing ability and exhibiting enzyme activity at oral pH levels.

The present disclosure relates generally to polypeptides capable of hydrolysing an amide bond in a polyamide, including polyamides of nylon polymers; methods of producing said polypeptides and uses thereof, including for hydrolysing said polyamide.

This invention discloses a high-throughput enzyme variant screening method based on a cross-attention graph convolutional neural network, relating to the fields of enzyme high-throughput screening technology and artificial intelligence bioinformatics. The invention establishes a prediction model, CEGCN, integrating the ESM-2 protein language model and a graph convolutional neural network. Utilizing bidirectional cross-attention to deeply couple sequence information with enzyme activity site map features, it performs high-throughput initial screening of 64 million enzyme variants with extremely low data dependence. A hierarchical physical filtering system is constructed, combining molecular docking, Rosetta energy analysis, and molecular dynamics simulations. By exploring the binding modes and dynamic stability of complexes, false positives are efficiently eliminated at the physical level, ensuring high fidelity of candidate variants. This method achieves initial screening through deep learning models and secondary screening through physical simulations, efficiently exploring a vast enzyme variant combinatorial space with minimal experimental data, providing an effective strategy for future high-throughput screening of other key industrial enzymes.

This application relates to: a novel ribophosphate diphosphate kinase variant polypeptide; a polynucleotide encoding the variant polypeptide; a microorganism comprising the variant polypeptide or the polynucleotide encoding the variant polypeptide; a method for producing L-amino acids, comprising the step of culturing the microorganism in a culture medium; and the use of the polypeptide, the polynucleotide, and the microorganism for the production of L-amino acids.

Disclosed herein, inter alia, are mutant enzymes, kits, and methods of use thereof.

The invention includes a mutant T7 DNA ligase or a biologically active fragment thereof, which has greater activity than wild type T7 DNA ligase. The mutant T7 DNA ligase, or the biologically active fragment, has one or more substitutions differing from the wild type, as described more fully in the Summary. The preferred mutant T7 DNA ligase has at least one of the following mutations: E63K (SEQ ID NO:4), K73E (SEQ ID NO:6), K137E (SEQ ID NO:7), K174E (SEQ ID NO:9), E182K (SEQ ID NO:11), K210E (SEQ ID NO: 13), E243K (SEQ ID NO:15), D245R (SEQ ID NO: 17), E268K (SEQ ID NO:19), E272K (SEQ ID NO:21), E289K (SEQ ID NO:23), K295E (SEQ ID NO:25) and D336R (SEQ ID NO:27).

The present disclosure provides a purine nucleoside enzyme variant, a nucleic acid sequence encoding the purine nucleoside enzyme variant, and further discloses a composition, a vector and a host cell comprising the purine nucleoside enzyme variant, and further provides a method for improving the efficiency of purine and / or D-ribose production.

This invention relates to a luciferase variant having a 35-80 amino acid deletion near the N-terminus of the sequence shown in SEQ ID NO.:1; preferably, the deletion is 35-40, 40-45, or 55-60 amino acids near the N-terminus of the sequence shown in SEQ ID NO.:1; the luciferase variant is configured to increase the luminescence intensity or caffeic acid content of an organism or its tissues or cells. This invention solves the problems of low luminescence efficiency and poor signal stability of the FBP system in organisms. This application systematically designs N-terminal truncated LUZ sequences of different lengths to screen for mutants that improve the luminescence effect of organisms. These mutants can be combined with other elements to further enhance the luminescence intensity of organisms.

The invention relates to bacteriophage encoded enzymes and enzyme variants having antimicrobial activity, to methods of making such enzymes and enzyme variants, and to bacteriostatic and bactericidal methods using such enzyme and enzyme variants.

The present invention relates to a novel zinc-binding dehydrogenase variant and a method of producing an L-aromatic amino acid using the same. The zinc-binding dehydrogenase variant is obtained by substituting one or more amino acids in the amino acid sequence constituting zinc-binding dehydrogenase to change the enzymatic activity of the zinc-binding dehydrogenase, and a recombinant microorganism comprising the variant is capable of efficiently producing an L-aromatic amino acid.

The present invention relates to a protease variant comprising an amino acid sequence which is at least 90% identical to SEQ ID NO: 1, or a fragment, fraction or shuffled variant thereof maintaining proteolytic activity, which protease variant has one or more amino acid substitutions, wherein at least one amino acid substitution is at residue position D447 of SEQ ID NO: 1, wherein the protease variant has increased thermostability compared to wildtype Kumamolisin Alicyclobacillus sendaiensis (Kumamolisin AS).

The present invention relates to lipase variants of a parent lipase having lipase activity, having at least 75% but less than 100% sequence identity to SEQ ID NO: 3, and comprising a substitution at one or more positions corresponding to positions 1, 2, 3, 4, 5, 6, 7, 9, 10, 11, 12, 16, 19, 30, 31, 34, 36, 37, 39, 40, 42, 44, 51, 52, 53, 54, 56, 58, 59, 70, 71, 72, 73, 83, 84, 86, 88, 90, 92, 93, 95, 96, 100, 101, 102, 104, 106, 109, 110, 112, 117, 119, 124, 125, 127, 128, 131, 132, 133, 134, 135, 137, 158, 159, 160, 161, 162, 163, 165, 166, 167, 168, 170, 181, 182, 183, 189, 190, 192, 194, 196, 202, 210, 211, 212, 220, 225, 227, 228, 229, 230, 231, 233, 237, 238, 239, 240, 242, 246, 247, 248, 252, 259, 262, 264, 269 of SEQ ID NO: 3. The present invention also relates to polynucleotides encoding these variants, nucleic acid constructs, vectors, and host cells comprising these polynucleotides, and methods of using these variants.