Purification and properties of a high-molecular-weight, alkaline exopolygalacturonase from a strain of Bacillus

被引：36

作者：

Kobayashi, T ^{[1
]}

Higaki, N ^{[1
]}

Suzumatsu, A ^{[1
]}

Sawada, K ^{[1
]}

Hagihara, H ^{[1
]}

Kawai, S ^{[1
]}

Ito, S ^{[1
]}

机构：

[1] Kao Corp, Tochigi Res Labs, Haga, Tochigi 3213497, Japan

来源：

ENZYME AND MICROBIAL TECHNOLOGY | 2001年 / 29卷 / 01期

关键词：

exopolygalacturonase; pectic enzyme; Bacillus;

D O I：

10.1016/S0141-0229(01)00355-6

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

An exopolygalacturonase [exo-PG; poly (1,4-alpha -D-galacturonide) digalacturonohydrolase, EC 3.2.1.82] was found in a culture of Bacillus sp. strain KSM-P576. The purified exo-PG had a molecular weight of approximately 115,000 and an isoelectric point of pH 4.6. The N-terminal amino acid sequence was Thr-Glu-Val-Ser-Pro-Lys-Ser-Pro-Ala-Ser-Pro-Val. Maximum activity toward polygalacturonic acid (PGA) was observed at 55 degreesC and pH 8.0 in 100 mM Tris-HCl buffer. The exo-PG was quite stable in various pH buffers between pH 6 and 12 when incubated at 30 degreesC for 1 h. Mg2+ Mn2+ Pd2+ and Ca2+ ions stimulated the enzyme activity. The exo-PG released digalacturonic acid from PGA, tri-, tetra-, and penta-galacturonic acids. The apparent K-m values for oligogalacturonic acids were almost identical, and k(cat) values increased with the chain length of the substrates. (C) 2001 Elsevier Science Inc. All rights reserved.

引用

页码：70 / 75

页数：6

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