{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1390282681449910656.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1271/bbb.64.447"}},{"identifier":{"@type":"COI","@value":"1:CAS:528:DC%2BD3cXhvVCjtb0%3D"}},{"identifier":{"@type":"PMID","@value":"10737210"}},{"identifier":{"@type":"NDL_BIB_ID","@value":"5296478"}},{"identifier":{"@type":"URI","@value":"http://id.ndl.go.jp/bib/5296478"}},{"identifier":{"@type":"URI","@value":"https://ndlsearch.ndl.go.jp/books/R000000004-I5296478"}},{"identifier":{"@type":"URI","@value":"http://www.tandfonline.com/doi/pdf/10.1271/bbb.64.447"}},{"identifier":{"@type":"NAID","@value":"110002679934"}}],"resourceType":"学術雑誌論文(journal article)","dc:title":[{"@language":"en","@value":"Purification and Characterization of a Family G/11 .BETA.-Xylanase from Streptomyces olivaceoviridis E-86."},{"@value":"Purification and Characterization of a Family G/11 β-Xylanase from Streptomyces olivaceoviridis E-86"},{"@language":"ja-Kana","@value":"Purification and Characterization of a Family G 11 ベータ Xylanase from Streptomyces olivaceoviridis E 86"},{"@value":"Purification and Characterization of a Family G/11 β-Xylanase from<i>Streptomyces olivaceoviridis</i>E-86"}],"dc:language":"en","description":[{"type":"abstract","notation":[{"@language":"en","@value":"A β-xylanase (GXYN) was purified from the culture filtrate of <i>Streptomyces olivaceoviridis</i> E-86 by successive chromatography on DE-52, CM-Sepharose and Superose 12. The molecular mass of the xylanase was estimated to be 23 kDa, indicating that the enzyme consists of a catalytic domain only. The enzyme dis- played an optimum pH of 6, a temperature optimum of 60°C, a pH stability range from 2 to 11 and thermal stability up to 40°C. The N-terminal amino acid sequence of GXYN was A-T-V-I-T-T-N-Q-T-G-T-N-N-G-I-Y-Y-S-F-W-, and sharing a high degree of similarity with the N-terminal sequence of xylanases B and C from <i>Streptomyces lividans</i>, indicating GXYN belongs to family G/11 of glycoside hydrolases. GXYN was inferior to xylanase B from <i>Streptomyces lividans</i> in the hydrolysis of insoluble xylan because of its lack of a xylan binding domain.<br>"}],"abstractLicenseFlag":"disallow"}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1410282681449910661","@type":"Researcher","foaf:name":[{"@language":"en","@value":"KANEKO Satoshi"}],"jpcoar:affiliationName":[{"@language":"en","@value":"National Food Research Institute, Ministry of Agriculture, Forestry, and 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Atsushi"}],"jpcoar:affiliationName":[{"@language":"en","@value":"Department of Material and Biological Chemistry, Faculty of Science, Yamagata University"},{"@language":"en","@value":"National Institute for Advanced Interdisciplinary Research"}]},{"@id":"https://cir.nii.ac.jp/crid/1410282681449910659","@type":"Researcher","personIdentifier":[{"@type":"NRID","@value":"9000004190319"}],"foaf:name":[{"@language":"en","@value":"MURAMATSU Mizuho"}],"jpcoar:affiliationName":[{"@language":"en","@value":"Institute of Applied Biochemistry, University of Tsukuba"}]},{"@id":"https://cir.nii.ac.jp/crid/1410282681449910656","@type":"Researcher","personIdentifier":[{"@type":"NRID","@value":"9000004190322"}],"foaf:name":[{"@language":"en","@value":"IWAMATSU Shinnosuke"}],"jpcoar:affiliationName":[{"@language":"en","@value":"Department of Material and Biological Chemistry, Faculty of Science, Yamagata 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Tsukuba"}]},{"@id":"https://cir.nii.ac.jp/crid/1410001204930233859","@type":"Researcher","personIdentifier":[{"@type":"NRID","@value":"9000002734986"},{"@type":"NRID","@value":"9000004119897"},{"@type":"NRID","@value":"9000004256838"},{"@type":"NRID","@value":"9000021261210"},{"@type":"NRID","@value":"9000401543605"},{"@type":"NRID","@value":"9000004169616"},{"@type":"NRID","@value":"9000014582917"},{"@type":"NRID","@value":"9000254277774"},{"@type":"NRID","@value":"9000021138656"},{"@type":"NRID","@value":"9000009453666"},{"@type":"NRID","@value":"9000021180844"},{"@type":"NRID","@value":"9000401544103"},{"@type":"NRID","@value":"9000401961541"},{"@type":"NRID","@value":"9000401960716"},{"@type":"NRID","@value":"9000021129428"},{"@type":"NRID","@value":"9000401543703"},{"@type":"NRID","@value":"9000004194876"},{"@type":"NRID","@value":"9000021129345"},{"@type":"NRID","@value":"9000401960307"},{"@type":"NRID","@value":"9000021148932"},{"@type":"NRID","@value":"9000300212810"},{"@type":"NRID","@value":"9000401543273"},{"@type":"NRID","@value":"9000322673408"},{"@type":"NRID","@value":"9000004229158"},{"@type":"NRID","@value":"9000004194868"},{"@type":"NRID","@value":"9000020796123"},{"@type":"NRID","@value":"9000283846185"},{"@type":"NRID","@value":"9000401960262"},{"@type":"NRID","@value":"9000252815270"},{"@type":"NRID","@value":"9000401544436"},{"@type":"NRID","@value":"9000253182815"},{"@type":"NRID","@value":"9000254277526"},{"@type":"NRID","@value":"9000401961183"},{"@type":"NRID","@value":"9000401960874"},{"@type":"KAKEN_RESEARCHERS","@value":"50353983"},{"@type":"NRID","@value":"1000050353983"},{"@type":"RESEARCHMAP","@value":"https://researchmap.jp/read4153"}],"foaf:name":[{"@language":"en","@value":"HAYASHI Kiyoshi"}],"jpcoar:affiliationName":[{"@language":"en","@value":"National Food Research Institute, Ministry of Agriculture, Forestry, and Fisheries"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"09168451"},{"@type":"EISSN","@value":"13476947"},{"@type":"NDL_BIB_ID","@value":"000000151899"},{"@type":"ISSN","@value":"09168451"},{"@type":"LISSN","@value":"09168451"},{"@type":"NCID","@value":"AA10824164"}],"prism:publicationName":[{"@language":"en","@value":"Bioscience, Biotechnology, and Biochemistry"},{"@language":"ja","@value":"Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ"},{"@language":"en","@value":"Biosci. Biotechnol. Biochem."},{"@language":"en","@value":"Bioscience, Biotechnology, and Biochemistry"},{"@language":"ja","@value":"Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ"}],"dc:publisher":[{"@language":"en","@value":"Japan Society for Bioscience, Biotechnology, and Agrochemistry"},{"@language":"ja","@value":"公益社団法人 日本農芸化学会"}],"prism:publicationDate":"2000","prism:volume":"64","prism:number":"2","prism:startingPage":"447","prism:endingPage":"451"},"reviewed":"false","dcterms:accessRights":"http://purl.org/coar/access_right/c_abf2","url":[{"@id":"http://id.ndl.go.jp/bib/5296478"},{"@id":"https://ndlsearch.ndl.go.jp/books/R000000004-I5296478"},{"@id":"http://www.tandfonline.com/doi/pdf/10.1271/bbb.64.447"}],"availableAt":"2000","foaf:topic":[{"@id":"https://cir.nii.ac.jp/all?q=family%20G/11%20xylanase","dc:title":"family G/11 xylanase"},{"@id":"https://cir.nii.ac.jp/all?q=purification","dc:title":"purification"},{"@id":"https://cir.nii.ac.jp/all?q=%3Ci%3EStreptomyces%20olivaceoviridis%3C/i%3E","dc:title":"<i>Streptomyces olivaceoviridis</i>"},{"@id":"https://cir.nii.ac.jp/all?q=%3Ci%3EStreptomyces%20lividans%3C/i%3E","dc:title":"<i>Streptomyces lividans</i>"},{"@id":"https://cir.nii.ac.jp/all?q=xylan%20binding%20domain","dc:title":"xylan binding domain"}],"relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1360855567871177216","@type":"Article","relationType":["cites"],"jpcoar:relatedTitle":[{"@value":"Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4"}]},{"@id":"https://cir.nii.ac.jp/crid/1390001204506789760","@type":"Article","relationType":["cites"],"jpcoar:relatedTitle":[{"@value":"菌体外放線菌キシラナーゼの精製とその諸性質"},{"@language":"en","@value":"Purification and Some Properties of Extracellular Xylanase from <i>Streptomyces</i> sp. E-86"},{"@language":"ja-Kana","@value":"キンタイガイ ホウセンキン キシラーゼ ノ セイセイ ト ソノ ショ セイシツ"}]},{"@id":"https://cir.nii.ac.jp/crid/1390001205362889600","@type":"Article","relationType":["isReferencedBy","isCitedBy"],"jpcoar:relatedTitle":[{"@language":"ja","@value":"【総説-受賞論文-】　糖質関連酵素の革新的な利用技術・改変技術の開発に関する研究"},{"@language":"en","@value":"[Review: Prize-awarded article] Research on the Development of Innovative Application and Modifying Technology for the Carbohydrate Relating Enzymes"},{"@value":"糖質関連酵素の革新的な利用技術・改変技術の開発に関する研究"},{"@language":"ja-Kana","@value":"トウシツ カンレン コウソ ノ カクシンテキ ナ リヨウ ギジュツ ・ カイヘン ギジュツ ノ カイハツ ニ カンスル ケンキュウ"}]},{"@id":"https://cir.nii.ac.jp/crid/1390001206474008320","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["cites"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Structure of Hardwood Xylan and Specificity of Streptomyces .BETA.-Xylanase toward the Xylan."},{"@value":"Structure of Hardwood Xylan and Specificity of<i>Streptomyces β</i>-Xylanase toward the Xylan"},{"@value":"Structure of hardwood xylan and specificity of Streptomyces β-xylanase toward the xylan"}]},{"@id":"https://cir.nii.ac.jp/crid/1390001206479036928","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Structure and Function of Carbohydrate-Binding Module Families 13 and 42 of Glycoside Hydrolases, Comprising a β-Trefoil Fold"},{"@value":"Award Review : Structure and Function of Carbohydrate-Binding Module Families 13 and 42 of Glycoside Hydrolases, Comprising a β-Trefoil Fold"}]},{"@id":"https://cir.nii.ac.jp/crid/1390282681268043136","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy","isCitedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Substrate Recognition of a Family 10 Xylanase from Streptomyces olivaceoviridis E-86: A Study by Site-directed Mutagenesis to Make an Hindrance around the Entrance toward the Substrate-binding Cleft"},{"@language":"ja","@value":"放線菌<i>Streptomyces olivaceoviridis</i> E-86由来ファミリー10キシラナーゼの基質認識"}]},{"@id":"https://cir.nii.ac.jp/crid/1390282681437082368","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["cites"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Preparation of glucuronoxylooligosaccharides from an acid hydrolysate of corn-hulls."}]},{"@id":"https://cir.nii.ac.jp/crid/1390282681441339904","@type":"Article","relationType":["cites"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Studies on the xylanase system of Streptomyces. 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Structures of the arabinoxylo-oligosaccharides from the hydrolytic products of corncob arabinoxylan by a xylanase from Streptomyces."},{"@value":"Structures of the arabinoxylo-oligosaccharides from the hydrolytic products of corn cob arabinoxylan by a xylanase from Streptomyces"}]},{"@id":"https://cir.nii.ac.jp/crid/1390282681448730624","@type":"Article","relationType":["cites"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Kinetic Studies on p-Nitrophenyl-cellobioside Hydrolyzing Xylanase from Cellvibrio gilvus."},{"@value":"Kinetic Studies on<i>p</i>-Nitrophenyl-cellobioside Hydrolyzing Xylanase from<i>Cellvibrio gilvus</i>"},{"@value":"Kinetic studies of p-nitrophenyl-cellobiose hydrolyzing xylanase from Cellvibrio gilvus"},{"@value":"Kinetic studies in p-nitrocellobioside hydrolyzing xylanase from Cellvibrio gilvus"}]},{"@id":"https://cir.nii.ac.jp/crid/1390282681454512000","@type":"Article","relationType":["isCitedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Purification and Characterization of a Thermostable Xylanase from Saccharopolyspora pathumthaniensis S582 Isolated from the Gut of a Termite"},{"@value":"Purification and Characterization of a Thermostable Xylanase from<i>Saccharopolyspora pathumthaniensis</i>S582 Isolated from the Gut of a Termite"}]},{"@id":"https://cir.nii.ac.jp/crid/1390585017622865792","@type":"Article","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Studies on Hemicellulases"},{"@language":"ja","@value":"ヘミセルラーゼに関する研究"}]},{"@id":"https://cir.nii.ac.jp/crid/1520573329850940160","@type":"Article","relationType":["cites"],"jpcoar:relatedTitle":[{"@value":"Crystallization and Preliminary X-Ray Crystallographic Study of Streptomyces olivaceoviridis E-86 β-Xylanase"},{"@language":"ja-Kana","@value":"Crystallization and Preliminary X-Ray C"}]},{"@id":"https://cir.nii.ac.jp/crid/1521136278509881856","@type":"Article","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Structural characterization of hemicellulose released from corn cob in continuous flow type hydrothermal reactor"}]},{"@id":"https://cir.nii.ac.jp/crid/1521980705635460480","@type":"Article","relationType":["cites"],"jpcoar:relatedTitle":[{"@value":"PCR Cloning and Expression of the F/10 Family Xylanase Gene from Streptomyces olivaceoviridis E-86"},{"@language":"ja-Kana","@value":"PCR Cloning and Expression of the F 10"}]},{"@id":"https://cir.nii.ac.jp/crid/1570291225877113216","@type":"Article","relationType":["cites"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Family-10 and family-11 xylanases differ in their capacity to enhance the bleachability of hardwood and softwood paper pulps."}]},{"@id":"https://cir.nii.ac.jp/crid/1570572699514233216","@type":"Article","relationType":["cites"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Remazol brilliant blue-xylan: a soluble chromogenic substrate for xylanases"}]},{"@id":"https://cir.nii.ac.jp/crid/1571417124053186048","@type":"Article","relationType":["cites"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Notes on sugar determination"}]},{"@id":"https://cir.nii.ac.jp/crid/1571417126660843008","@type":"Article","relationType":["cites"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Domains in microbial β-1,4-gly-canases : sequence conservation, function, and enzyme families"}]},{"@id":"https://cir.nii.ac.jp/crid/1572261551593967488","@type":"Article","relationType":["cites"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Sequences of three genes specifying xylanases in Streptomyces lividans."}]},{"@id":"https://cir.nii.ac.jp/crid/1573387448890666112","@type":"Article","relationType":["cites"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Protein measurement with the folin phenol reagent"}]},{"@id":"https://cir.nii.ac.jp/crid/1573668926467276032","@type":"Article","relationType":["cites"],"jpcoar:relatedTitle":[{"@language":"en","@value":"New families in the classification of glycosyl hydrolases based on amino acid sequence similarities"}]},{"@id":"https://cir.nii.ac.jp/crid/1574231874211471616","@type":"Article","relationType":["cites"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Cellulose-binding domains : classification and 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