Purification and characterization of thermostable chitinase from a novel S. maltophilia strain
Malaysian Journal of Microbiology
;
: 7-12, 2013.
Artigo
em Inglês
| WPRIM
| ID: wpr-626132
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 andResults:
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.
Texto completo:
DisponíveL
Índice:
WPRIM (Pacífico Ocidental)
Idioma:
Inglês
Revista:
Malaysian Journal of Microbiology
Ano de publicação:
2013
Tipo de documento:
Artigo
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