| http://purl.uniprot.org/citations/19605459 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19605459 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19605459 | http://www.w3.org/2000/01/rdf-schema#comment | "beta-1,3-Xylanase from Vibrio sp. strain AX-4 (XYL4) is a modular enzyme composed of an N-terminal catalytic module belonging to glycoside hydrolase family 26 and two putative carbohydrate-binding modules (CBMs) belonging to family 31 in the C-terminal region. To investigate the functions of these three modules, five deletion mutants lacking individual modules were constructed. The binding assay of these mutants showed that a repeating unit of the CBM was a non-catalytic beta-1,3-xylan-binding module, while the catalytic module per se was not likely to contribute to the binding activity when insoluble beta-1,3-xylan was used for the assay. The repeating CBMs were found to specifically bind to insoluble beta-1,3-xylan, but not to beta-1,4-xylan, Avicel, beta-1,4-mannan, curdlan, chitin or soluble glycol-beta-1,3-xylan. Both the enzyme and the binding activities for insoluble beta-1,3-xylan but not soluble glycol-beta-1,3-xylan were enhanced by NaCl in a concentration-dependent manner, indicating that the CBMs of XYL4 bound to beta-1,3-xylan through hydrophobic interaction. This property of the CBMs was successfully applied to the purification of a recombinant XYL4 from the cell extracts of Escherichia coli transformed with the xyl4 gene and the detection of beta-1,3-xylan-binding proteins including beta-1,3-xylanase from the extract of a turban shell, Turbo cornutus."xsd:string |
| http://purl.uniprot.org/citations/19605459 | http://purl.org/dc/terms/identifier | "doi:10.1093/jb/mvp108"xsd:string |
| http://purl.uniprot.org/citations/19605459 | http://purl.org/dc/terms/identifier | "doi:10.1093/jb/mvp108"xsd:string |
| http://purl.uniprot.org/citations/19605459 | http://purl.uniprot.org/core/author | "Araki T."xsd:string |
| http://purl.uniprot.org/citations/19605459 | http://purl.uniprot.org/core/author | "Araki T."xsd:string |
| http://purl.uniprot.org/citations/19605459 | http://purl.uniprot.org/core/author | "Ito M."xsd:string |
| http://purl.uniprot.org/citations/19605459 | http://purl.uniprot.org/core/author | "Ito M."xsd:string |
| http://purl.uniprot.org/citations/19605459 | http://purl.uniprot.org/core/author | "Kiyohara M."xsd:string |
| http://purl.uniprot.org/citations/19605459 | http://purl.uniprot.org/core/author | "Kiyohara M."xsd:string |
| http://purl.uniprot.org/citations/19605459 | http://purl.uniprot.org/core/author | "Yamaguchi K."xsd:string |
| http://purl.uniprot.org/citations/19605459 | http://purl.uniprot.org/core/author | "Yamaguchi K."xsd:string |
| http://purl.uniprot.org/citations/19605459 | http://purl.uniprot.org/core/author | "Sakaguchi K."xsd:string |
| http://purl.uniprot.org/citations/19605459 | http://purl.uniprot.org/core/author | "Sakaguchi K."xsd:string |
| http://purl.uniprot.org/citations/19605459 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19605459 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19605459 | http://purl.uniprot.org/core/name | "J. Biochem."xsd:string |
| http://purl.uniprot.org/citations/19605459 | http://purl.uniprot.org/core/name | "J. Biochem."xsd:string |
| http://purl.uniprot.org/citations/19605459 | http://purl.uniprot.org/core/pages | "633-641"xsd:string |
| http://purl.uniprot.org/citations/19605459 | http://purl.uniprot.org/core/pages | "633-641"xsd:string |
| http://purl.uniprot.org/citations/19605459 | http://purl.uniprot.org/core/title | "Characterization and application of carbohydrate-binding modules of beta-1,3-xylanase XYL4."xsd:string |
| http://purl.uniprot.org/citations/19605459 | http://purl.uniprot.org/core/title | "Characterization and application of carbohydrate-binding modules of beta-1,3-xylanase XYL4."xsd:string |
| http://purl.uniprot.org/citations/19605459 | http://purl.uniprot.org/core/volume | "146"xsd:string |
| http://purl.uniprot.org/citations/19605459 | http://purl.uniprot.org/core/volume | "146"xsd:string |