16 results about "Carbohydrate-binding module" patented technology

The invention relates to the field of enzyme engineering, in particular to modified xylanase, a DNA (deoxyribonucleic acid) molecule, a recombinant plasmid and a transfected cell. The modified xylanase protected by the application is formed by replacing a deletion segment of a receptor enzyme with a substitution segment, the receptor enzyme is wild type xylanase, the sequence of the receptor enzyme is SEQ ID NO: 1, the deletion segment comprises a carbohydrate binding module of the receptor enzyme, the substitution segment is a carbohydrate binding module of a donor enzyme, the donor enzyme is a carbohydrate active enzyme, and the donor enzyme is a carbohydrate active enzyme. The sequence of the donor enzyme is one of SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4 and SEQ ID NO: 5. The carbohydrate binding module of the carbohydrate active enzyme with relatively high activity is replaced into the receptor enzyme, so that the binding capacity of the receptor enzyme and the carbohydrate is improved, and the activity of the receptor enzyme is improved.

The invention discloses an endoglucanase truncated mutant and an application of the endoglucanase truncated mutant. According to the invention, based on endoglucanase BsEGL from bacillus subtilis DLG, a truncated mutant is constructed by deleting a carbohydrate binding domain (CBM) of the endoglucanase BsEGL, and the truncated mutant is named as BsEGL [delta] CBM. Compared with BsEGL, the truncated mutant BsEGL delta CBM has the advantages that the thermal stability, the pH stability, the organic solvent tolerance and the like are remarkably improved, and the activity of degrading phosphoric acid expanded cellulose and corncob xylan is obtained. In addition, the enzymatic activity of the truncated mutant BsEGL delta CBM is remarkably improved by 6.41%, and the catalytic efficiency is remarkably improved. Due to the characteristics, the mutant can be suitable for industrial processes such as feed processing, papermaking, biological energy sources, spinning and food brewing, and is particularly suitable for enzyme catalytic reaction under extreme environments such as high temperature and low pH. The invention provides an enzyme preparation tool with excellent performance for efficient degradation of cellulose biomass, and has important application value.

The present invention relates to isolated polypeptides having beta-glucanase activity, catalytic domains, carbohydrate binding modules and polynucleotides encoding the polypeptides, catalytic domains or carbohydrate binding modules. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides, catalytic domains or carbohydrate binding modules. The present invention further relates to processes for producing fermentation products from starch-containing or cellulosic-containing material, as well as an enzyme blend or composition, or a recombinant host cell or fermenting organism suitable for use in processes of the invention.

The present invention relates to polypeptides having mannanase activity, catalytic domains, and carbohydrate binding modules, and polynucleotides encoding the polypeptides, catalytic domains, and carbohydrate binding modules. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides, catalytic domains, and carbohydrate binding modules.

The invention provides a homogeneous immune FRET (Fluorescence Resonance Energy Transfer) analysis method and application of alginate, and belongs to the technical field of analytical chemistry and biosensing. The alginate fluorescent probe is prepared by respectively marking FRET donors and receptors on alginate by utilizing the high-specific recognition characteristic of a catalytic inactivated alginate lyase or carbohydrate binding module thereof on the alginate, and the probe is randomly combined on alginate molecules with a linear repetitive skeleton in a novel'sugar-coated haw 'structure. At an appropriate probe: alginate binding ratio, FRET donors and receptors are close to each other and generate FRET signals. The lanthanide complex is used as a fluorescence donor, and short-life background fluorescence interference in a biological sample is effectively filtered out by utilizing the long-life luminescence characteristic of the lanthanide complex. Compared with a conventional polysaccharide analysis method which usually needs a complex pretreatment process and relatively long detection time, the method disclosed by the invention can realize high-sensitivity, high-specificity, rapid and homogeneous immunofluorescence quantitative detection of algal polysaccharides in a biological sample.

The present application constructs a fusion protein by utilizing the specific affinity adsorption property of a carbohydrate binding module (CBM) to cellulose, the fusion protein comprising a cholesteric oxidase and a carbohydrate binding module (CBM), and then uses nanocellulose membranes as the immobilization carrier of the fusion protein for preparing a biosensor element, and the obtained biosensor element can exhibit good catalytic properties and detection stability.

The present invention relates to isolated polypeptides having alpha-amylase activity, polypeptides comprising an alpha-amylase catalytic domain and a carbohydrate binding module, and polynucleotides encoding the polypeptides, compositions comprising said polypeptides, as well as polynucleotides and nucleic acid constructs or vectors encoding the polypeptides, and host cells comprising the polynucleotides or constructs / vectors, as well as methods of producing and using the polypeptides.

A composition comprising a fusion protein (referred to as "sdAb-CBM: pSac") comprising a single domain antibody (sdAb) and a carbohydrate binding module (CBM) bound to a polysaccharide polymer by non-covalent binding of the polysaccharide polymer to the CBM, and its use for the prevention or treatment of infections caused by pathogens in the gastrointestinal tract.

The present invention relates to isolated polypeptides having xylanase activity, catalytic domains, and carbohydrate binding modules, as well as polynucleotides encoding these polypeptides, catalytic domains, or carbohydrate binding modules. The present invention also relates to nucleic acid constructs, vectors, and host cells comprising these polynucleotides, as well as methods for producing and using these polypeptides, catalytic domains, or carbohydrate binding modules.

Described herein is a reagent matrix comprising (a) a plurality of first capture components wherein the first capture component comprises a first analyte capture site; (b) a plurality of second capture components wherein the second capture component comprises a second analyte capture site and a cellulose binding domain (CBD) or carbohydrate binding module (CBM) wherein at least one of the first capture component or the second capture component comprises a detection medium; and (c) a plurality of cellulose nanofibrils. In one embodiment, the reagent matrix is combined with a porous substrate for detecting an analyte.

The application provides a fusion uric acid oxidase and application thereof in a biosensing element. The fusion uric acid oxidase comprises a carbohydrate binding module and a uric acid oxidase, and the fusion uric acid oxidase can be made into a biosensing element for uric acid detection, and has the advantages of high sensitivity and good stability.

The present application relates to the field of enzyme engineering, and more particularly to a modified xylanase, DNA molecule, recombinant plasmid, and transfected cells. The modified xylanase protected by the present application is formed by replacing a deleted segment of a receptor enzyme with a replacement segment. The receptor enzyme is a wild-type xylanase, the sequence of which is SEQ ID NO: 1. The deleted segment includes the carbohydrate-binding module of the receptor enzyme, and the replacement segment is the carbohydrate-binding module of a donor enzyme. The donor enzyme is a carbohydrate-active enzyme, and the sequence of the donor enzyme is one of SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, and SEQ ID NO: 5. By replacing the carbohydrate-binding module of a carbohydrate-active enzyme with a higher activity into the receptor enzyme, the receptor enzyme's ability to bind carbohydrates is improved, thereby increasing the activity of the receptor enzyme.

The present invention features thermostable protein binding scaffolds containing framework regions and variable loop regions that can be mutagenized to bind a desired target. The scaffolds are derived from the Carbohydrate Binding Module Family 32 (CBM32) protein domain of Clostridium perfringens hyaluronidase (NagH). The robust framework of the scaffolds described herein allows for the development of custom, high performance affinity chromatography resins compatible with the harsh conditions of process-scale applications that can be adaptable to a wide diversity of target substrates.

The invention belongs to the technical field of biology, and particularly relates to a carbohydrate binding module and application thereof. The invention discloses a carbohydrate binding module for the first time, and the carbohydrate binding module can be bound with insoluble polysaccharide and can be used for preparing and / or preparing tag protein, immobilizing target protein and / or preparing an immobilized compound.

The present invention relates to isolated polypeptides having xylanase activity, catalytic domains, carbohydrate binding modules and polynucleotides encoding the polypeptides, catalytic domains or carbohydrate binding modules. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides, catalytic domains or carbohydrate binding modules.

The present invention relates to cellobiohydrolase variants and carbohydrate binding module 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.