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Purification and gene cloning of a chitosanase from Bacillus ehimensis EAG1

Bacillus ehimensis EAG1 (IFO15659) produced and secreted chitosanase in the presence of exogenous chitosan. The chitosanase was purified from the culture filtrate of the bacterium to apparent homogeneity in SDS-polyacrylamide gel electrophoresis. The purified enzyme had a molecular weight of approxi...

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Bibliographic Details
Published in:Journal of bioscience and bioengineering 1999, Vol.87 (3), p.383-385
Main Authors: Akiyama, Kouichi, Fujita, Tadashi, Kuroshima, Ken-Ichi, Sakane, Takeshi, Yokota, Akira, Takata, Renkichi
Format: Article
Language:English
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Summary:Bacillus ehimensis EAG1 (IFO15659) produced and secreted chitosanase in the presence of exogenous chitosan. The chitosanase was purified from the culture filtrate of the bacterium to apparent homogeneity in SDS-polyacrylamide gel electrophoresis. The purified enzyme had a molecular weight of approximately 31,000. A 1.9-kbp DNA fragment containing the chitosanase gene was cloned and the complete nucleotide sequence was determined. The sequence was found to contain a single open reading frame encoding a protein of 302 amino acids. The deduced amino acid sequence showed significant homology with the chitosanase from Bacillus circulans MH-K1.
ISSN:1389-1723
1347-4421
DOI:10.1016/S1389-1723(99)80050-4