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Production and characterization of a thermostable chitinase from a new alkalophilic Bacillus sp. BG-11.

DIR@IMTECH: CSIR-Institute of Microbial Technology

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Title Production and characterization of a thermostable chitinase from a new alkalophilic Bacillus sp. BG-11.
 
Creator Bhushan, B
 
Subject QR Microbiology
 
Description An alkalophilic, environmental micro-organism, Bacillus sp. BG-11, has been isolated and characterized. It produced 76 U ml-1 of chitinase in liquid batch fermentation after 72 h of incubation at 50 degrees C using chitin-enriched medium. The molecular weight of purified chitinase was estimated to be 41 kDa by SDS-PAGE. The pH and temperature optima of chitinase immobilized on chitosan and calcium alginate were 8.5 and 50 degrees C, respectively, which were same as that of free enzyme. The pH and thermostability of immobilized chitinase were enhanced significantly. The chitinase immobilized on chitosan was stable between pH 5.0 and 10.0, and the half-life of chitosan-immobilized enzyme at 70, 80 and 90 degrees C was 90, 70 and 60 min, respectively. The end-products formed during the enzyme-substrate reaction were identified by 13C-NMR, and N-acetyl-D-glucosamine was found to be the major end-product. GlcNAc (GlcNAc)2 and (GlcNAc)3 inhibited the chitinase activity by 32, 25 and 18%, respectively, at a concentration of 10 mmol l-1. The shelf-life of chitinase (retained 100% activity) at 4 degrees C was 8 weeks in the presence of either sodium azide (100 microgram ml-1), sodium metabisulphite (0.1% w/v) or KCl (15% w/v). The enzyme was resistant to the action of proteases and allosamidin.
 
Publisher Wiley
 
Date 2000-05
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://crdd.osdd.net/open/320/1/bhushan2000.pdf
Bhushan, B (2000) Production and characterization of a thermostable chitinase from a new alkalophilic Bacillus sp. BG-11. Journal of applied microbiology, 88 (5). pp. 800-8. ISSN 1364-5072
 
Relation http://onlinelibrary.wiley.com/doi/10.1046/j.1365-2672.2000.01016.x/abstract
http://crdd.osdd.net/open/320/