PURIFICATION AND CHARACTERIZATION OF KERATINASE FROM HAIR-DEGRADING STREPTOMYCES ALBUS

The keratinase waste produced in large quantities all over the world from animals and birds including human beings. As the physiological and chemical methods of keratin degradation are not easy possible, the biological method has gained importance. The present study investigated purified keratinase from Keratinolytic Streptomyces albus. The cell-bound keratinolytic enzyme was purified 32.72-fold by gel filtration chromatography. The enzyme was characterized as a serine protease with a molecular mass of 29-35kD. Optimal activity pH and Temperature was measured at 7.0 and 400C furthermore, the various inhibitors had different effect on enzyme activity. PMSF and heavy metal ion HgCl2 were the most potent inhibitors and EDTA induced the activity by more than 135%, 2-mercaptoethanol did not show any impact on the enzyme, where pCMB, KCN, 8-hydroxyquinoline and cystine inhibited activity moderately.