熱凝固失活サイクロデキストリン合成酵素(CGTase)の再生

DOI

書誌事項

タイトル別名
  • Recovery of Enzyme Activity from Heat-treated Coagulated, CGTase
公開日
1997
DOI
  • 10.11541/jag1994.44.537
公開者
日本応用糖質科学会

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説明

Bacillus macerans cyclodextrin-producing enzyme (CGTase) was precipitated by the addition of trichloro acetic acid (TCA) at pH 2.1. After washing with water, dissolving in 0.1 N NaOH, adjusting the pH to 6.0, and freeze drying, powdered CGTase (p-CGTase) was prepared. p-CGTase was dissolved in a buffer and treated at various temperatures (50-100°C) to obtain a heat-treated coagulated protein (cp-CGTase). The protein was dissolved in an alkaline solution and neutralized with an acidic solution to pH 6.0, and the recovered activity was measured. The activity of p-CGTase was completely inactivated at over 70°C and the cyclodextrin-forming pattern of the recovered enzyme was not changed, but a considerable amount of activity was recovered using cp-CGTase; nearly 40% of activity was recovered after an 80°C treatment. It was infered that the free-enzyme protein is folded and coagulated to maintain activity at high temperature .

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詳細情報 詳細情報について

  • CRID
    1390282680146946944
  • NII論文ID
    130004257541
  • DOI
    10.11541/jag1994.44.537
  • COI
    1:CAS:528:DyaK1cXhtFKgsLg%3D
  • ISSN
    18844898
    13403494
  • データソース種別
    • JaLC
    • CiNii Articles
  • 抄録ライセンスフラグ
    使用不可

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