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
書誌事項
- タイトル別名
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- 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
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- 日本醸造協会誌
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日本醸造協会誌 93 (12), 990-997, 1998
公益財団法人 日本醸造協会
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詳細情報 詳細情報について
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- CRID
- 1390001206102123776
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- NII論文ID
- 130004306280
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- COI
- 1:CAS:528:DyaK1cXotFeqtrs%3D
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- ISSN
- 21864012
- 09147314
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- データソース種別
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- JaLC
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- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可