Purification and partial characterization of two extracellular keratinases of Scopulariopsis brevicaulis |
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Authors: | H K Malviya R C Rajak S K Hasija |
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Institution: | (1) Department of Biological Science, R.D. University, 482 001 Jabalpur, India |
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Abstract: | Two extracellular keratinases of Scopulariopsis brevicaulis were purified and partially characterized. The enzymes were isolated by the techniques of gel filtration chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). These keratinases (K I & K II) were purified approximately 33 and 29 fold, respectively. SDS-PAGE of the products of gel filtration chromatography (K I & II) produced only one band each, suggesting homogeneity. The optimum pH for both keratinases was 7.8, while the optimum temperatures were 40°C (K I) and 35°C (K II). Estimated molecular weights were 40–45 KDa and 24–29 KDa for K I & K II respectively. Both keratinases were inhibited by phenylmethylsulfonyl fluoride which suggests a serine residue at or near an active site. |
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Keywords: | S brevicaulis keratinase purification partial characterization |
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