BMB Reports | |
Overexpression and characterization of thermostable chitinase from Bacillus atrophaeus SC081 in Escherichia coli | |
Young Ju Choi^11  Eun Kyung Cho^12  In Soon Choi^23  | |
[1] Biological Science, College of Medical and Life Science, Silla University, Busan 617-736, Korea^3;Departments of^1;Food and Nutrition^2 | |
关键词: Acidic chitosan; | |
DOI : | |
学科分类:生物化学/生物物理 | |
来源: Korean Society for Biochemistry and Molecular Biology | |
【 摘 要 】
The chitinase-producing strain SC081 was isolated from Korean traditional soy sauce and identified as Bacillus atrophaeus based on a phylogenetic analysis of the 16S rDNA sequence and a phenotypic analysis. A gene encoding chitinase from B. atrophaeus SC081 was cloned in Escherichia coli and was named SCChi-1 (GQ360078). The SCChi-1 nucleotide sequences were composed of 1788 base pairs and 596 amino acids, which were 92.6, 89.6, 89.3, and 78.9% identical to those of Bacillus subtilis (ABG57262), Bacillus pumilus (ABI15082), Bacillus amyloliquefaciens (ABO15008), and Bacillus licheniformis (ACF40833), respectively. A recombinant SCChi-1 containing a hexahistidine tag at the amino- terminus was constructed, overexpressed, and purified in E. coli to characterize SCChi-1. H(6)SCChi-1 revealed a hydrolytic band on zymograms containing 0.1% glycol chitin and showed the highest lytic activity on colloidal chitin and acidic chitosan. The optimal temperature and pH for chitinolytic activity were 50°C and pH 8.0, respectively.
【 授权许可】
Unknown
【 预 览 】
Files | Size | Format | View |
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RO201910252001786ZK.pdf | 2361KB | download |