Isolation, Screening and Production Optimization of Keratinase Enzyme from Bacillus sp. Isolated from Chicken Feathers

Microbial keratinases have become increasingly important in biotechnology due to their ability to target the hydrolysis of highly rigid, strongly cross-linked structural polypeptide "Keratin". They are produced in a medium containing keratinous substrates such as feathers and hair, and belong to the group of serine proteases. This study focused on optimizing the isolation, screening, and production of keratinase enzymes from Bacillus sp. strains that were isolated from chicken feathers. Nine colonies were screened, and the K3 isolate showed the highest level of keratinase activity. The K3 isolate was identified as a Bacillus sp. bacterium based on its culture, morphology, and biochemical characteristics. To optimize the production of the keratinase enzyme, four different types of media were used, with feather meal broth producing the best results. The study also investigated the effect of physical factors such as pH and temperature on enzyme production, with the maximum production achieved at pH 7 and 50°C. The commercial importance of keratinase lies in their ability to produce cost-effective feather by-products for feeds and fertilizers, enzymatic dehairing for the leather and cosmetic industry, detergent uses, development of biopolymers from keratin fibers, enhancing drug delivery in some tissues, and hydrolysis of prion proteins. The findings of this study shows the potential of keratinase in various industrial applications, particularly in sustainable waste management, bioremediation, and the valorization of keratin-rich waste into valuable bioproducts.