SUBSITE STRUCTURE OF RHIZOPUS-NIVEUS GLUCOAMYLASE, ESTIMATED WITH THE BINDING PARAMETERS FOR MALTOOLIGOSACCHARIDES

被引：6

作者：

OHNISHI, M

机构：

[1] Department of Food Science and Technology., College of Agriculture, University of Kyoto, Kyoto City, 606, Sakyo‐ward

来源：

STARCH-STARKE | 1990年 / 42卷 / 08期

关键词：

D O I：

10.1002/star.19900420807

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

Based on Kd and Ki for maltosaccarides Gn (n = 1 ± 7) and on a specified mode of their binding, the intrinsic affinities A1, A2, –, Ai at subsites i (i = 1 ± 5), were tried to estimate for glucoamylase from Rhizopus niveus. Previously, we have evaluated the apparent values Ai using Km and k0 on the enzyme‐catalyzed hydrolysis for Gn, where A1 is nearly 0 kcal/mol. Thus A1, which was found here 3.3 kcal/mol, may be cancelled out with the heat, which is consumed for the hydrolytic cleavage of a substrate glucosyl bond. Copyright © 1990 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim

引用

页码：311 / 313

页数：3

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