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International Journal of Biological Chemistry
Year: 2007  |  Volume: 1  |  Issue: 3  |  Page No.: 174 - 178

Studies on Extra Cellular Enzyme Keratinase from Dermatophyte Microsporum gypseum

K.C. Raju, Ujjwal Neogi, Ruchi Saumya and N. Rajendra Goud    

Abstract: Keratinases (E.C. 3.4.4.25) are of particular interest because of their action on insoluble keratin substrates and generally on a broad range of protein substrates. The objective of this study is to isolation, screening, purification and determination of the enzymatic activity of extracellular keratinase from dermatophyte Microsporum gypseum. The study clearly indicates the presence of the enzyme keratinases in the dermatophyte Microsporum gypseum. One milliliter of the purified sample contain 80 μg of protein, 1.09 μmole mL-1 60 min enzyme activity and 13.6 μ mole mg-1 60 min specific activity with respect to the unpurified one. The purified and unpurified state of the enzyme was judged by SDS/PAGE. Purified enzyme showed a single band of molecular weight of 33 kDa. Characterization studies showed optimum activity at pH 8 and at 35°C. The enzyme kinetics increased with increased concentration of MgCl2 and decreasedwith increased concentration of ZnCl2. Maximum biomass and keratinase activity were observed from pH 7.0 to 9.0, which agrees with those described for most feather-degrading Bacillus. In this study, the optimum conditions for keratinase synthesis by the Microsporum gypseum were determined, which will be an essential step for the production of adequate amounts for application in research field and other areas.

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