title: Purification and partial characterization of two extracellular keratinases of Scopulariopsis brevicaulis.
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 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.
authors.affiliation: Department of Biological Science, R.D. University, Jabalpur, India.
authors.forename: H K
authors.initials: HK
authors.lastname: Malviya
authors.forename: R C
authors.initials: RC
authors.lastname: Rajak
authors.forename: S K
authors.initials: SK
authors.lastname: Hasija
mesh_terms: D002850:Chromatography, Gel; D004589:Electrophoresis, Disc; D004795:Enzyme Stability; D003904:Mitosporic Fungi / Q000201:enzymology*; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000737:chemistry* / Q000302:isolation & purification
chemical_list: D010447:Peptide Hydrolases; C035855:keratinase