著者

吉沢 淑 尾崎 裕子 武藤 敏昭 進藤 斉 角田 潔和 小泉 武夫

出版者

Brewing Society of Japan

雑誌

日本醸造協会誌 (ISSN:09147314)

巻号頁・発行日

vol.93, no.12, pp.990-997, 1998

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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 Mn<SUP>2+</SUP>. 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.