Purification and partial characterization of two extracellular keratinases ofScopulariopsis brevicaulis

✍ Scribed by H. K. Malviya; R. C. Rajak; S. K. Hasija

• Publisher: Springer Netherlands
• Year: 1992
• Tongue: English
• Weight: 486 KB
• Volume: 119
• Category: Article
• ISSN: 0301-486X
• DOI: 10.1007/bf00448814

✦ Synopsis

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 degrees C (K I) and 35 degrees 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.