Chitosanase activity of the enzyme previously reported as β-1,3-1,4-glucanase fromBacillus circulansWL-12
- 1 January 1998
- journal article
- research article
- Published by Taylor & Francis in Bioscience, Biotechnology, and Biochemistry
- Vol. 62 (11) , 2107-2114
- https://doi.org/10.1271/bbb.62.2107
Abstract
Chitosanases 33 kDa and 40 kDa in size were detected in the culture supernatant of Bacillus circulans WL-12. One of the two chitosanases, chitosanse 40 (40-kDa chitosanase) has been shown to be identical to the enzyme which has been reported previously as a beta-1,3-1,4-glucanase by Bueno et al. The enzyme has been classified into family 8 glycosyl hydrolases together with the enzymes formally known as cellulase family D. This enzyme named chitosanase 40/beta-1,3-1,4-glucanase hydrolyzed both chitosan and beta-1,3-1,4-glucan with similar efficiency. However, the production of the enzyme was induced with chitosan but not by beta-1,3-1,4-glucan. Therefore, it seems possible that the major substrate of this enzyme is chitosan rather than beta-1,3-1,4-glucan. Analysis of degradation products generated from partially N-acetylated chitosan showed that chitosanase 40/beta-1,3-1,4-glucanse hydrolyzes GlcN-GlcN and GlcN-GlcNAc linkages but not GlcNAc-GlcNAc nor GlcNAc-GlcN. The specificity for hydrolyzing linkages of this enzyme is similar to that of the chitosanase from S. griseus HUT6037.Keywords
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