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Genes (Basel). 2015 Dec 4;6(4):1268-82. doi: 10.3390/genes6041268.

Characterization of Thermotolerant Chitinases Encoded by a Brevibacillus laterosporus Strain Isolated from a Suburban Wetland.

Author information

1
College of Biological and Pharmaceutical Engineering, Wuhan Polytechnic University, Wuhan 430023, China. liunan3585@163.com.
2
College of Biological and Pharmaceutical Engineering, Wuhan Polytechnic University, Wuhan 430023, China. SG201302002@163.com.
3
College of Biological and Pharmaceutical Engineering, Wuhan Polytechnic University, Wuhan 430023, China. miaowhpu@126.com.

Abstract

To isolate and characterize chitinases that can be applied with practical advantages, 57 isolates of chitin-degrading bacteria were isolated from the soil of a suburban wetland. 16S rRNA gene analysis revealed that the majority of these strains belonged to two genera, Paenibacillus and Brevibacillus. Taking thermostability into account, the chitinases (ChiA and ChiC) of a B. laterosporus strain were studied further. Ni-NTA affinity-purified ChiA and ChiC were optimally active at pH 7.0 and 6.0, respectively, and showed high temperature stability up to 55 °C. Kinetic analysis revealed that ChiC has a lower affinity and stronger catalytic activity toward colloidal chitin than ChiA. With their stability in a broad temperature range, ChiA and ChiC can be utilized for the industrial bioconversion of chitin wastes into biologically active products.

KEYWORDS:

Brevibacillus laterosporus; chitinase; enzymatic properties; kinetic analysis

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