PURIFICATION AND PROPERTIES OF AN UNUSUALLY ACID-STABLE ENDO-POLYGALACTURONASE PRODUCED BY CORTICIUM ROLFSII

被引：38

作者：

KAJL, A

OKADA, T

机构：

[1] Department of Agricultural Chemistry, University of Kagawa, Kagawa-ken

来源：

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 1969年 / 131卷 / 01期

关键词：

D O I：

10.1016/0003-9861(69)90122-2

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A polygalacturonase has been purified 239 fold from the culture filtrate of Corticium rolfsii, and found to be a homogeneous protein by ultracentrifugal analysis. The enzyme is typical of an endo-polygalacturonase with a optimum for catalytic activity at pH 2.5. The enzyme is unusually acid-stable; even after storage at pH 1.5 and 20 ° for 72 hr, 93.5% of enzymic activity remains. The purified enzyme is active not only on oligo- and poly-galacturonic acids but also on pectin. In addition, the enzyme has macerating activity on several plant tissues. © 1969.

引用

页码：203 / &

共 22 条

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ENDO, A
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