44 results about "Carbohydrate-binding module" patented technology

The present invention relates to a hybrid enzyme comprising carbohydrate-binding module amino acid sequence and a fungal alpha-amylase amino acid sequence and to a variant of a fungal wild type enzyme comprising a carbohydrate-binding module and an alpha-amylase catalytic module. The invention also relates to the use of the hybrid enzyme or the variant in starch liquefaction.

The present invention relates to polypeptides comprising a carbohydrate-binding module amino acid sequence and,an alpha-amylase amino acid sequence as well as to the application of such polypeptides.

The present invention relates to polypeptides having glucoamylase activity and isolated polynucleotides encoding said polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods for producing and using the polypeptides. The invention also relates to the composition comprising a glucoamylase of the invention as well as the use such compositions for starch conversion processes, brewing, including processes for producing fermentation products or syrups.

The present invention relates to polypeptides comprising a carbohydrate-binding module amino acid sequence and an alpha-amylase amino acid sequence as well as to the application of such polypeptides.

The invention is related to a method and DNA constructs for obtaining in a filamentous fungus host a higher production level of a carbohydrate degrading (CD) enzyme, having in its original state a catalytic module (CAT) and a carbohydrate binding module (CBM) separated by a linker region. The DNA construct comprising a truncated actinomycetes, preferably Nonomuraea flexuosa (NJ) derived DNA sequence encoding a truncated form of the CD enzyme, for example Nf Xyn11A, Nf Xyn10A, and is introduced into a filamentous fungal host. Said CD enzyme contains the catalytically active region of CAT but lacks part or all of the CBM, or all of the CBM and part or all of the linker region and is expressed and secreted under the control of regulatory sequences comprising at least a signal sequence, but also promoters, terminators and DNA sequences encoding a secretable carrier protein or domains thereof, preferably originating from filamentous fungi are included. The production level obtained with DNA sequence having the shortened DNA sequence encoding the truncated form of the CD enzyme is higher than the production level obtained with DNA construct encoding the corresponding full length CD enzyme.

The invention provides a method of cellulose immobilized cis epoxy succinic acid hydrolase. The method comprises the following steps: fusing gene coding cis epoxy succinic acid hydrolase and carbohydrate binding module CMB30, efficiently expressing the fused gene in Escherichia coli, and then carrying out purification and immobilization on fused enzyme in crude enzyme liquid by adopting the cellulose. The invention also provides a method for catalyzing and hydrolyzing epoxy succinic acid to convert into L-tartaric acid or D-tartaric acid by adopting the cellulose immobilized cis epoxy succinic acid hydrolase as biocatalyst. The method has the beneficial effects that: not only is the stability of enzyme obviously improved, but also the cellulose used as purified and fixed substrate is low in price and easy to get by adopting the cellulose immobilized cis epoxy succinic acid hydrolase, and has excellent economic prospect. The method for preparing tartaric acid by adopting the cellulose immobilized cis epoxy succinic acid hydrolase has the advantages of reaction specificity, high product purity, high reaction efficiency and the like.

The invention relates to a high-temperature resisting neutral xylanase gene and engineering bacteria containing the gene. A gene sequence refers to a sequence 1, the whole length of the gene is 1134 bp and the gene is named as XynG1-1, the gene codes 377 amino acids, molecular weight of the gene is 41267 Da, wherein former 39 amino acids are signal peptide of the gene, the 49th to 235th amino acids are a conserved sequence of a glucosides hydrolase GH11 family, the 263rd to 377th amino acids are a conserved sequence of a carbohydrate-binding module CBM6 family. According to the invention, the recombinase obtained by fermenting the engineering bacteria has optimum temperature of 60 DEG C and optimum pH value of 7.0, heat is preserved at a pH value of 7.0 and temperature of 70 DEG C for 1 hour, the relative enzyme activity is more than 65%, and heat is preserved at a pH value of 9 and temperature of 60 DEG C for 1 hour, the relative enzyme activity is more than 60%. The xylanase of the present invention has the characteristic of good stability under high temperature, and can be applied to a plurality of industrial fields such as papermaking, foodstuff and forage, etc. The present invention has wide application prospect.

A polymer detection probe is provided that includes a binding module that specifically binds to at least one polymer and a reporter module that is spectroscopically detectable. The binding module can be a carbohydrate-binding module (CBM). The reporter module can be a fluorescent protein. A complex is provided that includes a probe specifically bound to a pulp or paper product including at least one surface available lignocellulosic polymer. A pulp or paper product is provided that includes at least one surface available lignocellulosic polymer and at least one probe bound thereto. Methods are provided that employ a lignocellulosic probe. A method of detecting a lignocellulosic polymer or other type of polymer is provided. A method of determining the effectiveness of an industrial treatment on pulp or a paper product is also provided. A method of determining a physical property of pulp or a paper product is further provided.

The invention discloses feruloyl esterase as well as mutants and application thereof. The feruloyl esterase has an amino acid sequence as shown in SEQ ID No. 1, SEQ ID No. 2 or SEQ ID No. 3, the feruloyl esterase is stable in property, the reaction pH is 6-8, and the reaction temperature is 37-54 DEG C. On the basis of the amino acid sequence of the feruloyl esterase, three feruloyl esterase mutants N.1-300, N.7-16 and N.9-98 are obtained by increasing the number of disulfide bonds in the feruloyl esterase, changing side chain groups of a carbohydrate binding module of the feruloyl esterase and changing the charges of a catalytic structural domain, and compared with original feruloyl esterase, the specific enzyme activities of the three mutants are obviously improved. The feruloyl esterase and the mutant obtained by the invention have stable properties, and are beneficial to industrial application of the feruloyl esterase.

The present invention relates to a novel xylanase homologous with an enzyme corresponding to a glycoside hydrolase family 10 (GH10) domain and comprising a carbohydrate-binding module family 2 (cellulose-binding module family 2, CBM2) domain, a substrate-binding module, which were isolated from Streptomyces sp. strain HY-14. Particularly, the maximum enzyme activity continues at at least 80% at a pH between 5.0 and 7.5 and the sugar substrates including xylans are significantly degraded in the xylanase, and thus the xylanase can be used as an enzyme in various industrial sectors such as food, feed, and other industries.

The present disclosure relates to isolated polynucleotides with two polynucleotide sequences linked within one open reading frame, in which the first polynucleotide sequence encodes a peptide that binds to a carbohydrate. The present disclosure also relates to vectors and genetically modified host cells containing such isolated polynucleotides and polypeptides encoded by such isolated polynucleotides. The present disclosure further relates to methods of increasing the ability of a recombinant protein to bind to a carbohydrate and methods of identifying a protein having an ability to bind to a carbohydrate.

The invention particularly relates to a fusion enzyme and application of the fusion enzyme in a paper-based biosensor. Glucose dehydrogenase (GDH) taking flavin adenine dinucleotide (FAD) as a coenzyme has good stability, is developed into a portable glucose sensor and has a good application prospect. The invention provides a GDH-linker-CBM fusion enzyme constructed by a flavin adenine dinucleotide (FAD) dependent glucose dehydrogenase (GDH) gene and a carbohydrate binding module (CBM) gene, and the GDH-linker-CBM fusion enzyme is prepared into a paper-based sensor through the modification effect of the carbohydrate binding module and a connecting peptide. The enzyme activity, the detection sensitivity and the anti-interference capability of the paper-based sensor are effectively improved, and a good market development prospect is realized.

The present invention relates to a hybrid polypeptide having alpha-amylase activity, selected from a first polypeptide sequence comprising a catalytic core, and a second polypeptide sequence comprising a carbohydrate binding module (CBM), wherein (a) the catalytic core is selected from a polypeptide having at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to amino acids 20 to 494 of SEQ ID NO: 1 or amino acids 20 to 496 of SEQ ID NO: 1; and (b) the CBM is selected from a polypeptide having at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity to SEQ ID NO: 4, SEQ ID NO: 5, or SEQ ID NO: 6. 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, and catalytic domains.

The invention relates to xylanase and particularly provides a heat-resistant xylanase and an application thereof. The heat-resistant xylanase can be: (a) a nucleic acid for encoding a polypeptide having xylanase activity, wherein a sequence of the protein that is encoded by the nucleic acid is represented as the amino sequence in SEQ ID No.2 (TM1); (b) a nucleic acid for encoding a polypeptide having xylanase activity, wherein the nucleic acid has a sequence having more than 80% homology with the SEQ ID No.2; or (c) a lacked signal sequence or a carbohydrate combination module of the xylanase that encoded by the nucleic acid in the (a) or (b). The xylanase TM1 and TM1-M has huge potential value in the applications of feeds, foods and pulping and papermaking industry.

A multifunctional polypeptide capable of hydrolyzing cellulosic materials, xylan, and mannan is disclosed. The polypeptide includes the catalytic core (cc) of Clostridium thermocellum Cthe_0797 (CelE), the cellulose-specific carbohydrate-binding module CBM3 of the cellulosome anchoring protein cohesion region (CipA) of Clostridium thermocellum (CBM3a), and a linker region interposed between the catalytic core and the cellulose-specific carbohydrate binding module. Methods of using the multifunctional polypeptide are also disclosed.