Identification, characterization and functional analysis of a GH-18 chitinase from Streptomyces roseolus

被引:30
作者
Jiang, Xiayun [2 ]
Chen, Daochun [2 ]
Hong, Shenle [2 ]
Wang, Weifen [2 ]
Chen, Shunshen [2 ]
Zou, Shuming [1 ]
机构
[1] Shanghai Ocean Univ, Key Lab Freshwater Aquat Genet Resources, Minist Agr, Shanghai 201306, Peoples R China
[2] Shanghai Ocean Univ, Coll Food Sci & Technol, Shanghai 201306, Peoples R China
基金
国家高技术研究发展计划(863计划); 美国国家科学基金会;
关键词
Chitinase; GH-18; Streptomyces; Antifungal activity; Chitinolysis; THERMOSTABLE CHITINASE; PROTOPLAST FORMATION; CYANEUS SP-27; PURIFICATION; GENE;
D O I
10.1016/j.carbpol.2011.11.008
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
A 40 kDa chitinase from Streptomyces roseolus DH was purified to homogeneity from culture medium. The N-terminal sequence was TPPPAKAVKLGYFTNWGVYG, which was highly homologous to the glycoside hydrolase (GH) 18 conserved domain of Streptomyces chitinases and included the two crucial Trp and Tyr sites. The purified enzyme showed maximal activity at 60 degrees C, pH 6.0 and exhibited good thermal and pH stabilities. The enzyme displayed strict substrate specificity on colloidal or glycol chitin, but not on chitosan derivatives. It was activated by Mg2+, Ba2+ and Ca2+, and inhibited by Cu2+, Co2+, Mn2+, whereas Zn2+ and ethylenediamine tetraacetic acid showed little inhibitory effects. Morphological changes observed by scanning electron microscopy revealed the occurrence of regular pores on the surface with the progress of enzymatic chitinolysis. Additionally, this GH-18 chitinase had a marked inhibitory effect on fungal hyphal extensions. In conclusion, this chitinase may have great potential for the enzymatic degradation of chitin. (C) 2011 Elsevier Ltd. All rights reserved.
引用
收藏
页码:2409 / 2415
页数:7
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