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Gene cloning and biochemical analysis of thermostable chitosanase (TCH-2) from Bacillus coagulans CK108

Authors
 Ho Geun Yoon, Kyung Han Lee, Hee Yun Kim, Hye Kyung Kim, Dong Hoon Shin, Bum Shik Hong , Hong Yon CHo 
Citation
 BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY, Vol.66(5) : 986-995, 2002 
Journal Title
 BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY 
ISSN
 0916-8451 
Issue Date
2002
Keywords
hermostable chitosanase ; Gene cloning ; Nucleotide sequencing ; Bacillus coagulans CK108 ; Chitosan oligosaccharide
Abstract
The DNA sequence of the thermostable chitosanase TCH-2 gene from Bacillus coagulans CK108 showed a 843-bp open reading frame that encodes a protein of 280 amino acids with a signal peptide corresponding to 32 kDa in size. The deduced amino acid sequence of the chitosanase from Bacillus coagulans CK108 has 61.6%, 48.0%, and 12.6% identities to those from Bacillus ehemensis, Bacillus circulans, and Bacillus subtilis, respectively. C-Terminal homology analysis shows that the enzyme belongs to the Cluster I group. The size of the gene was similar to those from mesophiles of the Cluster I group with regard to higher preference for codons ending in G or C. The recombinant chitosanase was electrophoretically purified to homogeneity by only two steps with column chromatography. The half-life of the enzyme was 40 min at 90°C. The purified protein was also highly stable, retaining above 50% residual activities during treatment with denaturants such as urea (8 M) and guanidine•HCl (4 M) at 37°C for 30 min. The enzyme had a useful reactivity and a high specific activity for producing functional oligosaccharides as well, producing the tetramer as a major product.
Files in This Item:
T200202146.pdf Download
DOI
10.1271/bbb.66.986
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Biochemistry and Molecular Biology (생화학-분자생물학교실) > 1. Journal Papers
Yonsei Authors
Yoon, Ho Geun(윤호근) ORCID logo https://orcid.org/0000-0003-2718-3372
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/143400
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