Abstract
A novel chitosanase gene, csn4, was identified through function-based screening of a marine mud metagenomic library. The encoded protein, named CSN4, which belonged to glycoside hydrolase family 46, showed its maximum identity (79%) with Methylobacter tundripaludum peptidoglycan-binding protein. CSN4 was expressed in Escherichia coli and purified. It displayed maximal activity at 30 °C and pH 7. A weakly-alkaline solution strongly inhibited the activity. The enzymatic activity was enhanced by addition of Mn2+ or Co2+. CSN4 exhibited strict substrate specificity for chitosan, and the activity was enhanced by increasing the degree of deacetylation. Thin-layer chromatography and electrospray ionization-mass spectrometry showed that CSN4 displayed an endo-type cleavage pattern, hydrolyzing chitosan mainly into (GlcN)2, (GlcN)3 and (GlcN)4. The novel characteristics of the chitosanase CSN4 make it a potential candidate to produce chitooligosaccharides from chitosan in industry.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: International Journal of Biological Macromolecules
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
