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

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.