International Journal of Environmental Sciences

Volume 4 Issue 4 2014- January 2014    Pages: 458-467  <<Previous    Next>>

Purification and Characterization of chitinase from Thermophilic Staphylococcus sp

Author Information:

Debalina Basu, Aditi Nag Chaudhuri

Lady Brabourne College, Calcutta University, P 1/2 Suhrawardi Avenue, Kolkata-17, West Bengal, India


The objective of the research was to study the purification and partial characterization of thermophilic chitinase from the newly isolated Staphylococcus sp. The enzyme was purified. The enzyme was of 66 kDa as was evident by native PAGE. The protein was showing activity at pH 7 and 9. The optimum temperature activity was 60°C. Influence of metal ions such as calcium chloride (CaCl2), Zinc sulfate (ZnSO4), Magnesium sulfate (MgSO4), Manganese sulfate (MnSO4) was observed. Substrate specificity of the enzyme was also studied. Phylogenetic tree of the producer organism was also done.

Keywords:-Chitinase, Thermophilic, Purification, Metal ions, 16S rDNA sequencing


© 2013 Copyright by the authors, licensee Integrated Publishing Association.This is an open access article distributed under the Creative Commons Attribution License (3.0) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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