清酒酵母の酢酸イソアミル分解酵素の性質 : 清酒酵母における酢酸イソアミル生成機構(第3報)

概要

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Isoamyl acetate hydrolytic enzyme was purified approximately 190-fold from the sake yeast Kyokai No. 7,by ammonium sulfate precipitation and column chromatography on DEAE-Sepharose, chromatofocusing, and gel filtration on Sephadex G-200. The molecular weight of the enzyme was about 48,000 by gel filtration on Sephadex G-200. the optimal temperature and pH of the enzyme activity were 30℃ and pH 7.5,respectively. The enzyme was stable between pH 5.0 and pH 8.0,but 50% of the activity was lost by standing at 40℃ for 15 min. The enzyme was most active for isobutyl acetate. Of the metal ions tested, Co^<2+> and Hg^<2+> were potent inhibitors of the enzyme activity. The enzyme was also inhibited by diisopropyl fluorophosphate. The enzyme appeared to be a carboxylesterase (EC3.1.1.1).
社団法人日本生物工学会の論文
1990-03-25