Malaysian Journal of Microbiology (Jan 2013)

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

  • Javed, S.,
  • Hamid, R.,
  • Abdin, Z.,
  • Ahmad, M. M.,
  • Ahmad, M.

Journal volume & issue
Vol. 9, no. 1
pp. 7 – 12


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Aims: The presents study examines the purification and characterization of a chitinase from S. maltophilia SJ602 strainisolated 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 andcolumn 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 and60 °C, respectively. Conclusion, Significance and Impact of the study: Besides showing a significant yield, the enzyme has a highthermal stability which has its applicability in the recycling of chitin waste.