Studies on the lceratinolytic enzymes of thermophilic Actinomycetes II-Partial purification and characterization of thermostable keratinase enzyme from Thermoactinomyces vulgaris C52

ABSTRACT

The thermostable keratinase enzyme, produced by Thermoacetinomyces vulgaris CS2 in liquid modified. Kosmatchev medium under the optimum condition, was purified 224-fold with an Overall yield of 36.08% of the original activity and specific activity 748.67 units mg [-1] protein by ammonium sulphate precipitation and ion exchange chromatography [DEAF-Cellulose]. Maximal activity of the enzyme was obtained at 55-60 and pH 8.4-85. It was stable at 45-55'in the pH 8.4-8.5. Also the enzyme was slightly activated by CaC12 MgSO4, FeSO4 and CuSO4, but strongly inhibited by KFeCN, KCN, iodine and iodoacedic acid. The partially purified enzyme actively hydrolyzed all keratinaceous waste materials used