Chitinase A from Stenotrophomonas maltophilia shows transglycosylation and antifungal activities

被引：52
作者：
Suma, Katta [1 ]
Podile, Appa Rao [1 ]
机构：
[1] Univ Hyderabad, Sch Life Sci, Dept Plant Sci, Hyderabad 500046, Andhra Pradesh, India
来源：
BIORESOURCE TECHNOLOGY | 2013年 / 133卷
关键词：
Chitooligosaccharides; Stenotrophomonas maltophilia; Chitinase; Transglycosylation; Antifungal activity; BIOLOGICAL-CONTROL; STRAIN; BINDING; PURIFICATION; DOMAIN; DEGRADATION; EXPRESSION; GENE;
D O I：
10.1016/j.biortech.2013.01.103
中图分类号：
S2 [农业工程];
学科分类号：
0828 ;
摘要：
Stenotrophomonas maltophilia chitinase (StmChiA and StmChiB) genes were cloned and expressed as soluble proteins of 70.5 and 41.6 kDa in Escherichia coli. Ni-NTA affinity purified StmChiA and StmChiB were optimally active at pH 5.0 and 7.0, respectively and exhibited broad range pH activity. StmChiA and StmChiB had an optimum temperature of 40 degrees C and are stable up to 50 and 40 degrees C, respectively. Hydrolytic activity on chitooligosaccharides indicated that StmChiA was an endo-acting enzyme releasing chitobiose and StmChiB was both exo/endo-acting enzyme with the release of GlcNAc as the final product. StmChiA showed higher preference to beta-chitin and exhibited transglycosylation on even chain length tetra- and hexameric substrates. StmChiA, and not StmChiB, was active on chitinous polymers and showed antifungal activity against Fusarium oxysporum. (C) 2013 Elsevier Ltd. All rights reserved.
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收藏
页码：213 / 220
页数：8
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