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  1. 紀要論文
  2. 琉球大学農学部学術報告
  3. 29号
  1. 部局別インデックス
  2. 農学部

クワズイモ葉のインベルターゼ(農芸化学科)

http://hdl.handle.net/20.500.12000/4027
http://hdl.handle.net/20.500.12000/4027
508882cb-062e-4bc1-9cde-284fb43b6de1
名前 / ファイル ライセンス アクション
KJ00000162136.pdf KJ00000162136.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 クワズイモ葉のインベルターゼ(農芸化学科)
言語 ja
タイトル
タイトル Invertase from Alocasia leaves(Department of Agricultural Chemistry)
言語 en
作成者 仲宗根, 洋子

× 仲宗根, 洋子

ja 仲宗根, 洋子

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安井, 勝

× 安井, 勝

ja 安井, 勝

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Nakasone, Yoko

× Nakasone, Yoko

en Nakasone, Yoko

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Yasui, Masaru

× Yasui, Masaru

en Yasui, Masaru

Search repository
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 クワズイモ葉のインベルターゼの調製方法としては, 硫安塩析よりもアセトン沈澱法が効果的であった。そこで, 20∿40%アセトン濃度で沈澱した, 部分精製の蛋白画分を, インベルターゼ酵素標品として用い, その諸性質を検討した。本酵素は至適pHが5.0でkm値が9mMの酸性インベルターゼであることが明らかとなった。本酵素は1mM水銀イオンによりほぼ完全に失活し, マンガンイオンおよびマグネシウムイオンの阻害をもうけた。また, 至適温度は35℃にあって, 15分間保持の45℃以上の温度ではほとんど活性を失なった。
内容記述
内容記述タイプ Other
内容記述 The paper reports the presence and some properties of acid invertase from Alocasia odora C. Koch leaves. Invertase activities for the protein fractions obtained by acetone, ethanol or ammonium sulfate precipitations were determined. The specific activities of acetone fraction, ethanol fraction and ammonium sulfate fraction were 11.9,14.3 and 2.2,respectively, indicating that the activities of the fractions obtained by the two organic solvents were about six times higher than that obtained by ammonium sulfate. Acetone fraction had an almost equivalent value to that of ethanol fraction in specific activity and the former had two times more than the latter in the content of enzyme protein. The fraction precipitated under 20-40% concentration of acetone, containing most of the invertase, was used for examination of the properties of the invertase from alocasia leaves. The invertase present in the leaves was acid invertase, having a pH optimum of 5.0 and almost no activity at alkaline areas. It had an optimum temperature of 35℃ and was inactivated at temperatures higher than 45℃. The enzyme was inhibited by the presence of 1 mM of Hg^<2+>, Mn^<2+> and Mg^<2+> and was not affected by that of Ca^<2+>, Fe^<2+>, Co^<2+> and K^+. The enzyme mainly showed β-fructofuranosidase activity with small level of maltase activity.
内容記述
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/20.500.12000/4027
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
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
収録物名
言語 en
収録物名 The Science Bulletin of the Faculty of Agriculture. University of the Ryukyus
書誌情報
号 29, p. 73-78, 発行日 1982-12-01
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