High efficient expression in Escherichia coli of chitinase gene cloned from Bacillus circulans C-2

Wang, Y. L., Zheng, H. W., Liu, X. L., Zhang, Y. Z. (July 1998) High efficient expression in Escherichia coli of chitinase gene cloned from Bacillus circulans C-2. Acta Biochimica Et Biophysica Sinica, 30 (4). pp. 352-356. ISSN 0582-9879

URL: https://www.ncbi.nlm.nih.gov/pubmed/12168036


Subcloning analysis of a cloned DNA fragment from Bacillus circulans containing the chitinase gene Chi1 showed that the chitinase gene lies on an 1.7 kb PstI-StyI fragment. The chitinase gene could be expressed in Escherichia coli strains JM107, DH5 alpha, XL1-blue and TG-1 with various efficiencies. The expression level of chitinase gene was highest in JM107, which was almost the same as that in B. circulans C-2. The molecular weight of extracellular chitinase was 66 kD by SDS-PAGE analysis. Cell location determination of the expressed chitinase showed that the enzyme existed not only in cell periplasm and cytoplasm, but also in extracellular broth. When the expression of the enzyme was optimal, the distribution of enzyme activity in extracellular broth, periplasm and cytoplasm was 35.8%, 32.1% and 32.9%, respectively.

Item Type: Paper
Subjects: Investigative techniques and equipment > cloning
Investigative techniques and equipment > assays > cloning
organism description > bacteria > escherichia coli
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > genes, structure and function > gene expression
CSHL Authors:
Communities: CSHL labs > Zheng lab
Depositing User: Matt Covey
Date: July 1998
Date Deposited: 22 Aug 2014 16:56
Last Modified: 24 Feb 2017 15:02
URI: https://repository.cshl.edu/id/eprint/30716

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