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  1. 紀要論文
  2. 琉球大学農学部学術報告
  3. 30号
  1. 部局別インデックス
  2. 農学部

細菌のアラビナン分解酵素の精製とその性質(農芸化学科)

http://hdl.handle.net/20.500.12000/3993
http://hdl.handle.net/20.500.12000/3993
16e384cb-23b6-4369-afda-b43b12293fe5
名前 / ファイル ライセンス アクション
KJ00000162167.pdf KJ00000162167.pdf
Item type デフォルトアイテムタイプ(フル)(1)
公開日 2008-02-14
タイトル
タイトル 細菌のアラビナン分解酵素の精製とその性質(農芸化学科)
言語 ja
作成者 安田, 正昭

× 安田, 正昭

ja 安田, 正昭

徳里, 政丈

× 徳里, 政丈

ja 徳里, 政丈

瀬底, 正康

× 瀬底, 正康

ja 瀬底, 正康

Yasuda, Masaaki

× Yasuda, Masaaki

en Yasuda, Masaaki

Tokuzato, Masatake

× Tokuzato, Masatake

en Tokuzato, Masatake

Sesoko, Masayasu

× Sesoko, Masayasu

en Sesoko, Masayasu

アクセス権
アクセス権 open access
アクセス権URI http://purl.org/coar/access_right/c_abf2
内容記述
内容記述タイプ Other
内容記述 土壌から分離した細菌のアラビナン分解酵素の精製を行ない, その性質を検討した。酵素の精製は, Bacillus sp. No. 430の培養ろ液から硫酸アンモニウム分画, DEAE-セルロース, QAE-セファデックスA-50,DEAE-トーヨーパール650S, ヒドロキシアパタイト及びセファデックスG-75などのカラムクロマトグラフィーを組み合わせて行なった。精製酵素はディスク電気泳動的に高度に精製されていた。精製酵素の反応至適pHは6.5,反応至適温度は40℃であった。精製酵素はビートアラビナン, アラビノガラクタン, アラビノキシランやp-nitrophenyl α-L-arabinofuranosideに作用した。反応生成物はL-アラビノースのみが検出された。本精製標品はα-L-arabinofuranosidaseであると考えられた。
内容記述タイプ Other
内容記述 This study was carried out for a purpose of effective utilization of agricultural wastes by microbial enzymes. In order to liberate arabinose from arabinose-containing polysaccharides such as arabinan, arabinoxylan and arabinogalactan, an α-L-arabinofuranosidase was investigated. An α-L-arabinofuranosidase I was purified from the culture fluid of Bacillus sp. No. 430,which was isolated from the soil of sugar-cane fields. The process was as follows; salting out by ammonium sulfate, DEAE-cellulose, QAE-Sephadex A-50,DEAE-Toyopearl 650 S, hydroxyapatite and Sephadex G-75 column chromatography. The enzyme was highly purified by the method of discelectrophoresis. The purified enzyme had the maximum reactivity at pH 6.5 and 40℃. The highly purified enzyme was confirmed to be able to liberate L-arabinose from beet arabinan, arabinogalactan, arabinoxylan and p-nitrophenyl α-L-arabinofuranoside. The reaction product was paper chromatographically demonstrated to be only L-arabinose. The purified enzyme was inactive for p-nitrophenyl β-D-galctopyranoside.
内容記述タイプ Other
内容記述 紀要論文
出版者
言語 ja
出版者 琉球大学農学部
言語
言語 jpn
資源タイプ
資源タイプ departmental bulletin paper
資源タイプ識別子 http://purl.org/coar/resource_type/c_6501
出版タイプ
出版タイプ VoR
出版タイプResource http://purl.org/coar/version/c_970fb48d4fbd8a85
識別子
識別子 http://hdl.handle.net/20.500.12000/3993
識別子タイプ HDL
収録物識別子
収録物識別子タイプ ISSN
収録物識別子 0370-4246
収録物識別子タイプ NCID
収録物識別子 AN00250548
収録物名
言語 ja
収録物名 琉球大学農学部学術報告
書誌情報
号 30, p. 201-209
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