SUBSTRATE-SPECIFICITY OF A NEUTRAL ALPHA-GLUCOSIDASE FROM PIG SERUM

被引：9

作者：

CHIBA, S ^{[1
]}

HIBI, N ^{[1
]}

SHIMOMURA, T ^{[1
]}

机构：

[1] HOKKAIDO UNIV, FAC AGR, DEPT AGR CHEM, SAPPORO, HOKKAIDO 060, JAPAN

来源：

AGRICULTURAL AND BIOLOGICAL CHEMISTRY | 1976年 / 40卷 / 09期

关键词：

D O I：

10.1080/00021369.1976.10862296

中图分类号：

S3 [农学（农艺学）];

学科分类号：

090104 [作物信息科学与技术];

摘要：

The substrate specificity of a neutral .alpha.-glucosidase was investigated. The enzyme was especially active on malto-oligosaccharides, phenyl-.alpha.-maltoside and nigerose. The action on isomaltose and phenyl-.alpha.-glucoside was too weak. Isomalto-oligosaccharides made up of 3 or more glucose units were not attacked. The .alpha.-glucans, such as amylopectin, .beta.-limit dextrin, glycogen and amylose besides soluble starch, were also hydrolyzed. The ratio of velocity of hydrolysis for maltose, nigerose, phenyl-.alpha.-maltoside, maltotriose and maltotetraose was estimated to be 100:89:93:74:80 in this order. The extraporated Km values for maltose, nigerose, phenyl-.alpha.-maltoside, maltotriose and maltotetraose were 2.1 mM, 20.0 mM, 0.33 mM, 0.28 mM and 0.15 mM, respectively. The enzyme is considered to be essentially a neutral .alpha.-glucosidase with a preferential activity on malto-oligosaccharides.

引用

页码：1813 / 1817

页数：5

共 15 条

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[2]

SUBSTRATE-SPECIFICITY OF NEUTRAL ALPHA-GLUCOSIDASE FROM RABBIT MUSCLE [J].