Purification and characterization of thermostable chitinase from a novel S. maltophilia strain

Aims: The presents study examines the purification and characterization of a chitinase from S. maltophilia SJ602 strain isolated from a soil sample collected from Jamia Hamdard, New Delhi. Methodology and Results: The purification steps included chitin affinity using colloidal chitin as the affinity matrix and column chromatography using Sephadex G-100. The chitinase was purified to 66 fold having a yield of 17%. The molecular weight of the chitinase was found to be around 29 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The pH and temperature optima of the purified chitinase were found to be at pH 5.5 and 60 °C, respectively. Conclusion, Significance and Impact of the study: Besides showing a significant yield, the enzyme has a high thermal stability which has its applicability in the recycling of chitin waste.