Fractionation of isozymes and determination of the subsite structure of glucoamylase from Rhizopus niveus.
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- TANAKA Akiyoshi
- Department of Food Science and Technology, Faculty of Agriculture, Kyoto University Present address: Department of Chemistry, Faculty of Education, Mie University
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- FUKUCHI Yoshikazu
- Department of Food Science and Technology, Faculty of Agriculture, Kyoto University
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- OHNISHI Masatake
- Department of Food Science and Technology, Faculty of Agriculture, Kyoto University
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- HIROMI Keitaro
- Department of Food Science and Technology, Faculty of Agriculture, Kyoto University
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- AIBARA Shigeo
- Research Institute for Food Science, Kyoto University
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- MORITA Yuhei
- Research Institute for Food Science, Kyoto University
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Four isozymes of glucoamylase were isolated from a commercial preparation of the enzyme from Rhizopus niveus by ion-exchange chromatography on CM-Sephadex C-50 and/or the preparative isoelectric focusing method on Sephadex IEF.<br> The kinetic parameters, Michaelis constant Km and molecular activity k0, for the hydrolysis of maltooligosaccharides (degree of polymerization DP from 2 to 7) were determined on the major component enzyme at pH 4.5 and 25°C. It was found that Km decreases and k0 increases with increasing DP. From the DP-dependences of Km and k0, the subsite affinities of the seven subsites of the enzyme active site were evaluated on the basis of subsite theory. These values are very similar to those obtained for an unfractionated preparation of Rhizopus delemar glucoamylase [Hiromi et al, B. B. A., 302, 362 (1973)].
収録刊行物
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- Agricultural and Biological Chemistry
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Agricultural and Biological Chemistry 47 (3), 573-580, 1983
公益社団法人 日本農芸化学会
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詳細情報 詳細情報について
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- CRID
- 1390001206465660672
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- NII論文ID
- 130000027554
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- COI
- 1:CAS:528:DyaL3sXhslGmtL4%3D
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- ISSN
- 18811280
- 00021369
- http://id.crossref.org/issn/00021369
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- Crossref
- CiNii Articles
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- 使用不可