メロン酒原料夕張メロン果肉のプロテアーゼの精製と諸性質

DOI

書誌事項

タイトル別名
  • Purification and Characterization of Protease Isolated from the Sarcocarp of Yubari Melon Fruit

抄録

A protease was purified from the sarcocarp of Yubari melon fruit, the raw material used in the production of melon wine, by a series of treatments consisting of ammonium sulfate precipitation, gel filtration and ion-exchange chromatography. The enzyme was a monomer protein without a carbohydrate moiety. Its characteristics are as follws: molecular weight 66 kDa, isoelectric point pH 8.5, optimal temperature 40°C, and enzyme activity is promoted in the presence of Mn2+. It is a characterisric serine protease and preferentially hydrolyzes peptide bonds on the carboxyl terminal side of Phe and Arg.<BR>The sequence of the N termcnal 20 amcno acods was determined.

収録刊行物

  • 日本醸造協会誌

    日本醸造協会誌 93 (12), 990-997, 1998

    公益財団法人 日本醸造協会

詳細情報 詳細情報について

  • CRID
    1390001206102123776
  • NII論文ID
    130004306280
  • DOI
    10.6013/jbrewsocjapan1988.93.990
  • COI
    1:CAS:528:DyaK1cXotFeqtrs%3D
  • ISSN
    21864012
    09147314
  • データソース種別
    • JaLC
    • Crossref
    • CiNii Articles
  • 抄録ライセンスフラグ
    使用不可

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