{"created":"2023-06-19T11:38:40.412053+00:00","id":6427,"links":{},"metadata":{"_buckets":{"deposit":"d757ec3a-81f3-4629-bbee-90c46a14e606"},"_deposit":{"created_by":13,"id":"6427","owners":[13],"pid":{"revision_id":0,"type":"depid","value":"6427"},"status":"published"},"_oai":{"id":"oai:mie-u.repo.nii.ac.jp:00006427","sets":["515:516:517:518"]},"author_link":["14946","14947"],"item_4_biblio_info_6":{"attribute_name":"書誌情報","attribute_value_mlt":[{"bibliographicIssueDates":{"bibliographicIssueDate":"2010-10-01","bibliographicIssueDateType":"Issued"},"bibliographicIssueNumber":"2","bibliographicPageEnd":"4","bibliographicPageStart":"1","bibliographic_titles":[{"bibliographic_title":"Proceedings of the Second International Workshop on Regional Innovation Studies :  (IWRIS2010)"}]}]},"item_4_description_14":{"attribute_name":"フォーマット","attribute_value_mlt":[{"subitem_description":"application/pdf","subitem_description_type":"Other"}]},"item_4_description_4":{"attribute_name":"抄録","attribute_value_mlt":[{"subitem_description":"The recombinant endoglucanase of family 44\n(Cel44A) isolated from Clostridium thermocellum F1 has activities\nfor cellulase, xylanase, and xyloglucanase. Previous studies\nusing mutant Cel44A (E186Q) had suggested that Trp64\nplay a crucial role in binding to cellooligosaccharides. This\nstudy confirmed previous findings, and provided further studies\nunderstanding the role of each subsite in the cleft of the\ncatalytic domain. Isothermal titration calorimetry (ITC)\nprovided a direct measure of binding enthalpy (ΔH) and allowed\nthe determination of the association constants (Ka) of\nthe mutated Cel44As with various degrees of cellooligosaccharides.\nExperimental binding studies with the mutants lacking\naromatic binding residues (W64A/E186Q and\nW64A/Y71A/E186Q) suggest that the each amino acid residues\ndidn’t dominate whole enzymatic affinity. However,\nW64A/E186Q and W64A/Y71A/E186Q showed a higher affinity\nfor cellohexaose and cellopentaose than did E186Q. These\nhigh affinities are probably seemed to be related to the rates of\nhydrolysis and product pattern as demonstrated by enzyme\nassay and thin layer chromatography of hydrolytic products.\nOur result suggests that the high affinity of catalytic domain\ncauses its products to remain in the cleft and delay the proceeding\nof hydrolysis.","subitem_description_type":"Abstract"}]},"item_4_publisher_30":{"attribute_name":"出版者","attribute_value_mlt":[{"subitem_publisher":"Graduate School of Regional Innovation Studies, Mie University"}]},"item_4_text_65":{"attribute_name":"資源タイプ（三重大）","attribute_value_mlt":[{"subitem_text_value":"Departmental Bulletin Paper / 紀要論文"}]},"item_4_version_type_15":{"attribute_name":"著者版フラグ","attribute_value_mlt":[{"subitem_version_resource":"http://purl.org/coar/version/c_970fb48d4fbd8a85","subitem_version_type":"VoR"}]},"item_creator":{"attribute_name":"著者","attribute_type":"creator","attribute_value_mlt":[{"creatorNames":[{"creatorName":"Kanie, M.","creatorNameLang":"en"}],"nameIdentifiers":[{"nameIdentifier":"14946","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Karita, S.","creatorNameLang":"en"}],"nameIdentifiers":[{"nameIdentifier":"14947","nameIdentifierScheme":"WEKO"}]}]},"item_files":{"attribute_name":"ファイル情報","attribute_type":"file","attribute_value_mlt":[{"accessrole":"open_date","date":[{"dateType":"Available","dateValue":"2017-02-18"}],"displaytype":"detail","filename":"60C15222.pdf","filesize":[{"value":"587.5 kB"}],"format":"application/pdf","licensetype":"license_note","mimetype":"application/pdf","url":{"label":"60C15222.pdf","url":"https://mie-u.repo.nii.ac.jp/record/6427/files/60C15222.pdf"},"version_id":"5afef556-eff0-4540-882b-48fe8ca44a2c"}]},"item_keyword":{"attribute_name":"キーワード","attribute_value_mlt":[{"subitem_subject":"cellulase / ITC","subitem_subject_scheme":"Other"}]},"item_language":{"attribute_name":"言語","attribute_value_mlt":[{"subitem_language":"eng"}]},"item_resource_type":{"attribute_name":"資源タイプ","attribute_value_mlt":[{"resourcetype":"departmental bulletin paper","resourceuri":"http://purl.org/coar/resource_type/c_6501"}]},"item_title":"The Relationship Between The Affinity and The Kinetics of Cellulase for Its Substrate","item_titles":{"attribute_name":"タイトル","attribute_value_mlt":[{"subitem_title":"The Relationship Between The Affinity and The Kinetics of Cellulase for Its Substrate","subitem_title_language":"en"}]},"item_type_id":"4","owner":"13","path":["518"],"pubdate":{"attribute_name":"PubDate","attribute_value":"2011-11-04"},"publish_date":"2011-11-04","publish_status":"0","recid":"6427","relation_version_is_last":true,"title":["The Relationship Between The Affinity and The Kinetics of Cellulase for Its Substrate"],"weko_creator_id":"13","weko_shared_id":-1},"updated":"2023-09-19T06:23:23.194800+00:00"}