%0 Journal Article
%T Purification and characterization of thermostable chitinase from a novel S. maltophilia strain
%A Hamid
%A R.
%A Ahmad
%A M.
%A Ahmad
%A M. M.
%A Abdin
%A Z.
%J Malaysian Journal of Microbiology
%D 2013
%I Malaysian Society for Microbiology
%X 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 ˇăC, 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.
%K Chitinase
%K S. maltophilia
%K Chitin affinity
%K Chitinase purification
%U http://web.usm.my/mjm/issues/vol9/Research%202.pdf