{"title":"酵母菌双乙酰还原酶的分离纯化及某些性质的研究。","authors":"A V Kavadze, A K Rodopulo, G L Shaposhnikov","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>A highly active preparation of diacetyl(acetoin) reductase was isolated from cell-free extracts of the yeast Saccharomyces vini. Since the activity ratio of 2,3-butanediol dehydrogenase and diacetyl(acetoin) reductase was practically unchanged in the process of 65-fold purification, it can be assumed that the yeast cells contain one enzyme, which catalyzes both the reversible oxidation of 2,3-butanediol to acetoin by NAD and the practically irreversible reduction of diacetyl to acetoin by NAD-H2. Some properties of this enzyme were studied.</p>","PeriodicalId":9166,"journal":{"name":"Biology bulletin of the Academy of Sciences of the USSR","volume":"6 3","pages":"356-61"},"PeriodicalIF":0.0000,"publicationDate":"1979-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Isolation, purification, and study of certain properties of diacetyl(acetoin) reductase in the yeast Saccharomyces vini.\",\"authors\":\"A V Kavadze, A K Rodopulo, G L Shaposhnikov\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>A highly active preparation of diacetyl(acetoin) reductase was isolated from cell-free extracts of the yeast Saccharomyces vini. Since the activity ratio of 2,3-butanediol dehydrogenase and diacetyl(acetoin) reductase was practically unchanged in the process of 65-fold purification, it can be assumed that the yeast cells contain one enzyme, which catalyzes both the reversible oxidation of 2,3-butanediol to acetoin by NAD and the practically irreversible reduction of diacetyl to acetoin by NAD-H2. Some properties of this enzyme were studied.</p>\",\"PeriodicalId\":9166,\"journal\":{\"name\":\"Biology bulletin of the Academy of Sciences of the USSR\",\"volume\":\"6 3\",\"pages\":\"356-61\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1979-05-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biology bulletin of the Academy of Sciences of the USSR\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biology bulletin of the Academy of Sciences of the USSR","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Isolation, purification, and study of certain properties of diacetyl(acetoin) reductase in the yeast Saccharomyces vini.
A highly active preparation of diacetyl(acetoin) reductase was isolated from cell-free extracts of the yeast Saccharomyces vini. Since the activity ratio of 2,3-butanediol dehydrogenase and diacetyl(acetoin) reductase was practically unchanged in the process of 65-fold purification, it can be assumed that the yeast cells contain one enzyme, which catalyzes both the reversible oxidation of 2,3-butanediol to acetoin by NAD and the practically irreversible reduction of diacetyl to acetoin by NAD-H2. Some properties of this enzyme were studied.
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