SUBSTRATE COMPETITION AND SPECIFICITY AT THE ACTIVE-SITE OF AMYLOPULLULANASE FROM CLOSTRIDIUM-THERMOHYDROSULFURICUM

被引：37

作者：

MATHUPALA, S

SAHA, BC

ZEIKUS, JG

机构：

[1] MICHIGAN STATE UNIV,DEPT MICROBIOL & PUBL HLTH,E LANSING,MI 48824

[2] MICHIGAN BIOTECHNOL INST,LANSING,MI 48909

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1990年 / 166卷 / 01期

关键词：

D O I：

10.1016/0006-291X(90)91920-N

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 highly thermostable pullulanase purified from Clostridium thermohydrosulfuricum strain 39E displayed dual activity with respect to glycosidic bond cleavage. The enzyme cleaved α-1,6 bonds in pullulan, while it showed α-1,4 activity against malto-oligosaccharides. Kinetic analysis of the purified enzyme in a system which contained both pullulan and amylose as the two competing substrates were used to distinguish the dual specificity of the enzyme from the single substrate specificity known for pullulanases and α-amylases. © 1990.

引用

页码：126 / 132

页数：7

共 20 条

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