45 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.

The present invention relates to variants of a parent lipase, wherein said variants have at least 60% but less than 100% sequence identity to SEQ ID NO: 2, have lipase activity, the variants comprise a substitution at a position corresponding to position 92 and / or 96 of SEQ ID NO: 2; and are unchanged at positions corresponding to positions 231, 233 and 254 of SEQ ID NO: 2. The present invention also relates to polynucleotides encoding these variants, nucleic acid constructs, vectors, and host cells comprising the polynucleotides, and methods of using the variants.

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 provides to an improved high-throughput system and method for generated and screening of genetic variants by combinatorial modifications. Also provided are optimized SpCas9 enzyme variants produced by this system.

The present invention relates to a method for estimating or determining fitness of enzyme variants and / or optimizing a nucleotide sequence encoding an enzyme variant comprising generating a DNA variant library and linking a unique DNA barcode to each DNA variant, wherein the DNA variants are subjected to long-read and short-read sequencing. In particular, the present invention relates to a method for predicting or determining fitness of enzyme variants and / or optimizing a nucleotide sequence encoding an enzyme variant by combining DNA barcodes, selection pressure, long-read sequencing, and short-read sequencing. Furthermore, the present invention relates to application of machine learning for predicting enzyme fitness and / or optimizing a nucleotide sequence encoding an enzyme variant based on data obtained from said method.

The present disclosure relates to an isopropylmalate synthase variant and a method of producing L-leucine using the same.

The present invention relates to a novel ABC transporter permease variant and a method for producing 5 '-inosinic acid using the same. The ABC transporter permease variant has a modified protein activity due to the substitution of one or more amino acids in the amino acid sequence constituting the ABC transporter permease, and thus a recombinant microorganism comprising the ABC transporter permease variant can efficiently produce 5 '-inosinic acid.

The present invention relates to a protein engineering technology that enhances the enzyme activity of human hyaluronidase, a hyaluronic acid hydrolase, at neutral pH, and more particularly to a novel hyaluronidase mutant or section thereof, comprising one or more amino acid residue substitutions in or near the enzyme active site of the amino acid sequence of the natural hyaluronidase Hyal1 (SEQ ID NO: 1), and selectively cleaving additional N-terminal and / or C-terminal amino acid residues.

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.

The invention discloses an editor fusing 5 'exonuclease and CRISPR-Cas12i2 as well as construction and application of the editor, and relates to the technical field of plant biology. The editor for fusing the 5'exonuclease and the CRISPR-Cas12i2 comprises a 5 'exonuclease T5E and Cas12i2 variant fusion protein T5E-Cas12i2 v1 coded by a nucleotide sequence, and a nuclear localization signal bpNLS, the 5' exonuclease T5E, the Cas12i2 variant Cas12i2 v1 and a nuclear localization signal bpNLS are sequentially arranged from the N end to the C end. Compared with an existing plant genome editing tool, the constructed T5E-Cas12i2v1 editor has the advantages that the efficiency is high, TTN-PAM sites are targeted, and site-specific large fragment deletion can be generated. The method is beneficial to accurate manipulation research on large cis-genetic elements, and has a wide application prospect in plant functional genome research and genetic improvement of crops.

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.

The invention provides a T4 DNA ligase variant which has increased T / A connection specificity, in the library construction process, the library yield and the library quality can be improved by using the T4 DNA ligase variant, and the A / T separation problem in offline data is solved to a certain extent.

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 invention relates to variants of a parent lipase which has lipase activity and comprise one or more substitutions corresponding to G23S, D27N, A40I, F51I,L, E56R, D57N, V60E,K, K98I, N101D, R118F, G163S, T231R, N233R, Y220F, T244E, and P256T using SEQ ID NO: 2 for numbering. The present invention also relates to compositions or microcapsule compositions comprising a lipase variant of the invention and to liquid products comprising a microcapsule composition of the invention as well as the use of said microcapsule composition for stabilizing lipase variants of the invention.

The application discloses a Trichoderma reesei engineering bacterium for secreting and expressing egg white lysozyme and a construction method thereof, and belongs to the field of molecular biology and biotechnology. The application firstly provides an egg white lysozyme mutant, and the amino acid sequence is shown in any one of SEQ ID NO. 2-4. The construction method of the Trichoderma reesei engineering bacterium for secreting and expressing egg white lysozyme comprises the following steps: taking Trichoderma reesei as a starting strain, and transforming an expression module into the Trichoderma reesei to construct the Trichoderma reesei engineering bacterium; the expression module comprises a promoter, a secretion peptide gene, an egg white lysozyme gene and a terminator which are sequentially connected. By transforming the coding gene of the egg white lysozyme into the Trichoderma reesei genome, the Trichoderma reesei engineering strain for secreting and expressing egg white lysozyme is successfully constructed. It is found that different egg white lysozyme variants can bring different effects, and when the Trichoderma reesei RUT-C30 is used as the starting strain, the effect is better than that of QM6a.

The present invention relates to polypeptide having alpha-amylase activity. The present invention also relates to polynucleotides encoding the polypeptides; nucleic acid constructs, vectors, and host cells comprising the polynucleotides; and methods of using the polypeptides.

The invention relates to TEV protease, in particular to a TEV protease variant and application thereof. The invention provides a TEV protease mutant, the nucleotide sequence of the TEV protease mutant is shown as SEQ.ID.2, and the amino acid sequence of the TEV protease mutant is shown as SEQ.ID.4. According to the invention, a gene of a TEV mutant is integrated into a pET28b vector and is transformed into a BL21 competent cell for expression, and protein is purified through IMAC (immobilized metal chromatography) and SEC (molecular exclusion chromatography). The TEV mutant shows higher expression quantity which is increased by 6 times compared with wild type TEV, meanwhile, the thermal stability and the activity of the TEV mutant are also improved, and part of protease is still remained after the TEV mutant is quickly heated at 95 DEG C, and the activity is still kept.

A method for making intermediate compounds suitable for making muscenone, the compositions made by said methods, the various uses of said compositions, and enzyme variants useful in said methods.

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.

Provided is a parent phytase variant, which relates to the technical field of protein engineering. The variant, relative to the parent phytase thereof, has one or more amino acid substitutions at positions corresponding to positions 295, 349, and 374 of SEQ ID NO: 1. Compared to the parent phytase, the variant has increased thermal stability.

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.

Provided is a parent phytase variant, which relates to the technical field of protein engineering. The variant, relative to the parent phytase thereof, has one or more amino acid substitutions at positions corresponding to positions 295, 349, and 374 of SEQ ID NO: 1. Compared to the parent phytase, the variant has increased thermal stability.