Exopolygalacturonate lyase from a thermophilic Bacillus sp.

被引：48
|
作者：
Singh, SA [1 ]
Plattner, H [1 ]
Diekmann, H [1 ]
机构：
[1] Leibniz Univ Hannover, Inst Mikrobiol, D-30167 Hannover, Germany
来源：
ENZYME AND MICROBIAL TECHNOLOGY | 1999年 / 25卷 / 3-5期
关键词：
exopolygalacturonate lyase; thermostable enzyme; purification; Bacillus licheniformis;
D O I：
10.1016/S0141-0229(99)00066-6
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 endospore-forming bacterial strain that was isolated from the hot extract of su,oar beet and identified as a strain of Bacillus licheniformis excretes an active 38-kDa exopolygalacturonate lyase. The enzyme was purified to homogeneity by ammonium sulfate precipitation, gel filtration, hydrophobic interaction chromatography, and ion-exchange chromatography. The pH optimum of the enzyme was found to be 11.0 and the temperature optimum, 69 degrees C. Its activity is dependent on Ca2+; 100% activity was retained at 65 degrees C after 2 h. The N-terminal sequence was determined and found to contain the motif GFAALNGGTTGG in accordance with the motif G(aro)a(S-7x)TxGG in other pectate lyases of the pelADE and pelBC families. 4,5-Unsaturated trigalacturonate was released as the product by the action of the enzyme. (C) 1999 Elsevier Science Inc. All rights reserved.
引用
收藏
页码：420 / 425
页数：6
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