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The Surfactant-Induced Conformational and Activity Alterations in Rhizopus Niveus Lipase

The Surfactant-Induced Conformational and Activity Alterations in Rhizopus Niveus Lipase

Parvez Alam, Gulam Rabbani, Gamal Badr, Badr Mohamed Badr, Rizwan Hasan Khan

Cell Biochem Biophys. 2015 Mar;71(2):1199-206.

PMID: 25424356

Abstract:

In this study, we have reported the effect of nonionic, anionic, cationic, and zwitterionic detergents on the enzymatic activity and structural stability of Rhizopus niveus lipase. Secondary structural changes were monitored by Far-UV CD which shows that surfactant induces helicity in the Rhizopus niveus lipase protein which was maximum in case of CTAB followed by SDS, CHAPS, and Brij-35. Similarly, tertiary structural changes were monitored by tryptophan fluorescence. We also carried out enzyme kinetics assays which showed that activity was enhanced by 1.5- and 1.1-fold in the presence of CHAPS and Brij-35, respectively. Furthermore, there was a decline in activity by 20 and 30 % in case of SDS and CTAB, respectively. These studies may be helpful in understanding detergent-lipase interaction in greater detail as lipases are used in many industrial processes.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP9001621-G	Lipase from Rhizopus niveus		9001-62-1	Price

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