Some Properties of an Invertase-liberating Enzyme Isolated from Zymolyase
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概要
- 論文の詳細を見る
An enzyme which released invertase from cell ghosts of Candida utilis was isolated in an electrophoretically pure state from "Zymolyase." The molecular weight of the purified enzyme was estimated to be 5.8 x 104, and its isoelectric point was pH 6.9. The enzyme was stable in a pH range from 6.0 to 9.0, and the optimal pH for liberation of invertase from cell ghosts was around 6.0. The activity of the enzyme was competitively inhibited by glucose, mannose, and sucrose. Unlike the starting enzyme preparation, "Zymolyase, " the purified enzyme released invertase without making holes on the surface of the cell ghosts. Various tests were applied, but the specificity of the enzyme was not defined.
- 社団法人 日本農芸化学会の論文
著者
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Iizuka Masaru
Faculty Of Science Osaka City University
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Yamamoto Takehiko
Faculty Of Engineering Fukuyama University
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TORII Yasuhiko
Faculty of Science, Osaka City University
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