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Updated: Jun 7, 2026

Measurement of Chitinase Activity in Biological Samples
Published on: August 22, 2019
Chitobiose production by using a novel thermostable chitinase from Bacillus licheniformis strain JS isolated from a
Shailesh R Waghmare1, Jai S Ghosh
1Department of Microbiology, Shivaji University, Vidyanagar, Kolhapur 416 004, India.
Abstract:
The thermophilic Bacillus licheniformis strain JS was isolated from a bed of mushrooms, Pleurotus sajor-caju. The organism could produce a novel, single-component, thermostable chitinase that was purified by ion-exchange chromatography using DEAE-cellulose in 7.64% yield and in an 8.1-fold enhancement in purity. Its molecular weight is 22kDa. The enzyme is a chitobiosidase, since the chitin hydrolysate is N(I),N(II)-diacetylchitobiose. The optimum temperature for enzyme activity is 55°C, and the optimum pH is 8.0. It was completely inhibited by Hg(2+) ions whereas Co(2+) ions served as an activator. The thermostability of this enzyme is important in the bioconversion of chitinous waste and for the production of chitooligosaccharides.
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