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Overexpression and characterization of thermostable chitinase from Bacillus atrophaeus SC081 in Escherichia coli
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  • Overexpression and characterization of thermostable chitinase from Bacillus atrophaeus SC081 in Escherichia coli
  • Overexpression and characterization of thermostable chitinase from Bacillus atrophaeus SC081 in Escherichia coli
저자명
Cho. Eun-Kyung,Choi. In-Soon,Choi. Young-Ju
간행물명
BMB reports
권/호정보
2011년|44권 3호|pp.193-198 (6 pages)
발행정보
생화학분자생물학회
파일정보
정기간행물|ENG|
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이 논문은 한국과학기술정보연구원과 논문 연계를 통해 무료로 제공되는 원문입니다.
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기타언어초록

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. $H_6SCChi$-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 $50^{circ}C$ and pH 8.0, respectively.