20 results about "Carbohydrate-binding protein" patented technology

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 invention relates to a pair of anti-TSH receptor (TSHR) autoantibody-binding fusion proteins consisting of a capture fusion protein and a detection fusion protein, and a method for detecting autoantibodies to the thyroid stimulating hormone receptor (TSHR) in a biological fluid sample, which employs said fusion proteins pair. More specifically, the capture and detection fusion proteins of the pair of the invention comprise an extracellular domain of a human TSHR and a monomeric non-human immunoglobulin Fc domain, or fragment thereof, or a bacterial maltose binding protein (MBP). Also disclosed is a kit for carrying out the method of the invention. In a preferred embodiment, the method of the invention is a sandwich immunoassay.

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 invention relates to a pair of anti-TSH receptor (TSHR) autoantibody-binding fusion proteins consisting of a capture fusion protein and a detection fusion protein, and a method for detecting autoantibodies to the thyroid stimulating hormone receptor (TSHR) in a biological fluid sample, which employs said fusion proteins pair. More specifically, the capture and detection fusion proteins of the pair of the invention comprise an extracellular domain of a human TSHR and a monomeric non-human immunoglobulin Fc domain, or fragment thereof, or a bacterial maltose binding protein (MBP). Also disclosed is a kit for carrying out the method of the invention. In a preferred embodiment, the method of the invention is a sandwich immunoassay.

The present invention provides a modified protein sequence, namely a recombinantly expressed glycan-binding protein. This glycan-binding protein is a variant of the Sclerotium Rolfsii lectin and has been modified to include features such as increased molecular stability, a reduction in N-terminal methionine impurities, and improved protein conjugation with other biological and chemical agents.

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 invention provides a novel streptococcus group A oligosaccharide antigen and glycobinding protein vaccine, which is characterized in that oligosaccharide antigen containing 30-70% of N-acetyl glucamine multi-rhamnose core skeleton structure is accurately prepared through chemical synthesis, and is efficiently coupled with KLH (the loading capacity is about 215 oligosaccharide / KLH molecules); safe, efficient and broad-spectrum immune protection is realized; safety: the GlcNAc side chain modification design avoids autoimmune risks (such as acute rheumatic fever heat); high efficiency: the animal experiment antibody titer reaches 1: 12, 800; the broad spectrum is as follows: the highly conservative universal GAS oligosaccharide antigen can universally cover various serotypes, and the key synthetic route (Scheme 2, 3, 16 and 20, the yield is 22%-96%) and the loading capacity verification (HPAEC) support the technical feasibility.

The present invention relates to Actinomycetales strains for the improved formation of acarbose. Provided are Actinomycetales strains which are engineered to overexpress dTDP-D-glucose-4,6-dehydratase (AcbB) and / or uridyltransferase (GtaB). Also provided are Actinomycetales strains which are engineered to have a reduced or absent expression of the small carbohydrate binding protein (Cgt) and / or a reduced or absent expression of genes which are essential for carotenoid synthesis. Also provided are tools, methods and means to generate these strains.

Disclosed is an alternate method of prevention and treatment of diseases caused by viral pathogens of human being and animals including coronaviruses, influenza viruses, etc., by food supplementation or fortification of food with foodstuff derived from transgenic plants or parts thereof obtained from the presently disclosed transgenic plant seed. This method provides said transgenic plant seed, wherein the genome of said seed comprises an exogenous recombinant polynucleotide encoding a combination of polypeptides, which are carbohydrate binding proteins, particularly lectins that in combination as disclosed herein are combined in a manner to overcome potential toxicity caused by their transgenic expression and to lower the concentrations of each of the carbohydrate binding proteins when expressed as a part of the combination when compared to the individual transgenic expression of any of said carbohydrate binding proteins, and wherein said seed exhibit inhibition of viral replication and provide immunity against viral pathogens.

The present invention aims to provide a fucose-binding protein that shows improved productivity in cases of expression in a host such as Escherichia coli, improved binding affinity to a fucose-containing sugar chain such as a sugar chain containing a structure composed of Fucα1-2Galβ1-3GlcNAc and / or Fucα1-2Galβ1-3GalNAc, and / or improved thermal stability. The above object is achieved by deleting a plurality of amino acid residues in the C-terminal side of the amino acid sequence of the fucose-binding protein BC2LCN of SEQ ID NO: 1, and, when necessary, substituting the glycine residue at position 36 in SEQ ID NO: 1 with a cysteine residue, substituting the glutamine residue at position 39 in SEQ ID NO: 1 with a leucine residue or methionine residue, substituting the glutamine residue at position 65 in SEQ ID NO: 1 with a leucine residue, substituting the cysteine residue at position 72 in SEQ ID NO: 1 with a glycine residue or alanine residue, substituting the glutamic acid residue at position 81 in SEQ ID NO: 1 with a cysteine residue, glutamine residue, histidine residue, or methionine residue, and / or substituting the glycine residue identified as the residue at position 36 in SEQ ID NO: 1 with a cysteine residue.

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.

Disclosed are methods, systems, components, and compositions for cell-free synthesis of glycosylated proteins, which may be utilized in vaccines, including anti-bacterial vaccines. The glycosylated proteins may include a bacterial polysaccharide conjugated to a carrier, which may be utilized to generate an immune response in an immunized host against the polysaccharide conjugated to the carrier. Suitable carriers may include but are not limited to Haemophilus influenzae protein D (PD), Neisseria meningitidis porin protein (PorA), Corynebacterium diphtheriae toxin (CRM 197), Clostridium tetani toxin (TT), and Escherichia coli maltose binding protein, and variants thereof.

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 discloses a method for identifying glycosyltransferase or glycosidase specific enzyme participating in DNA / RNA glycosylation, which is characterized in that oxidation labeling is carried out on glycosylation modification of DNA / RNA molecules, and solid phase coupling and enzyme digestion strategies are combined, so that enzyme or sugar binding protein specifically bound with glycosylation DNA / RNA can be efficiently and accurately captured, and the specific enzyme of glycosyltransferase or glycosidase can be identified. The interference caused by non-specific binding is obviously reduced. The method is not only suitable for various biological samples including tissue slices, blood and cell samples, but also compatible with subsequent mass spectrometric analysis, and high-throughput identification and function annotation of targeted proteins are realized. The technology provides a brand new tool for analyzing the action mechanism of DNA / RNA sugar modification in epigenetic regulation and control, and has important value for promoting the research of related disease mechanisms and the development of targeted therapy strategies.

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 application provides a kind of nanobody specifically binding maltose binding protein and application, belong to the field of biotechnology.Nanobody can recognize the new epitope on MBP different from maltose binding pocket, so its binding with MBP is not affected by the presence or absence of maltose.This makes the purification process can be carried out in the buffer containing maltose, and elution without adding maltose, significantly simplify the process and avoid foreign sugar pollution, realize the efficient purification without sugar elution, stable protein complex formation and target protein release under mild conditions, significantly improve the applicability and reliability of MBP fusion protein in purification, structure analysis and function research.

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.

The invention discloses application of carbohydrate binding protein BnaCARB in regulation and control of thousand seed weight, and belongs to the technical field of genetic engineering. The invention provides an application of a carbohydrate binding protein BnaCARB or a coding gene thereof, or a related biological material of the coding gene in regulation and control of thousand seed weight of rape or cultivation of high-yield rape. Research finds that BnaCARB genes (BnaA09.CARB and BnaC08. CARB) in oilseed rape can regulate and control the thousand seed weight of the oilseed rape, the thousand seed weight of the oilseed rape can be remarkably increased by knockout mutants of the genes, the thousand seed weight of the oilseed rape can be increased by utilizing the genes, and high-yield oilseed rape germplasm can be obtained. The invention provides a theoretical basis for further in-depth study on the physiological mechanism of rape yield, also provides genetic resources and technical support for creation and cultivation of high-yield rape germplasm, and has very important application prospects in breeding and improvement of high-yield rape varieties.