Proteinase K activities from talaromyces flavus, with respect to its keratin hydrolyzing enzymes

ABSTRACT

Keratinolytic proteinase K is secreted by Talaromyces flaves in a media containing Goat hairs, as carbon and nitrogen sources. Maximal proteinase production was obtained at pH 605 after 9 days incubation at 28§ +/- under shaking condition. The enzyme was purified from the cell free filtrate of the culture by applying [NH4]2SO4 precipitation and performing sephadex G 200 column. Two proteinase A and B were obtained, the first with a purification folds 23 and the second with 38. It's purity was tested by applying the poly acrylamide gel electrophoresis. The molecular weight of the enzyme [s] was determined, [A] 31, 500 and [B] 36, 750. Its stability against storage, temperature, buffers, pH and different substrates was also tested