Purification and characterization of thermostable chitinase from a novel S. maltophilia strain
- Author:
Rifat Hamid
;
Mahboob Ahmad
;
Malik M. Ahmad
;
M. Z. Abdin
;
Saleem Javed
- Publication Type:Journal Article
- Keywords:
Chitinase, S. maltophilia, chitin affinity, chitinase purification
- From:Malaysian Journal of Microbiology
2013;9(1):7-12
- CountryMalaysia
- Language:English
-
Abstract:
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.
- Full text:P020160926355920668114.pdf
