Abstract
Paecilomyces lilacinus strain PL-HN-16 was found to have the ability to degrade feathers. During the degradation process, the broth initially turned as sticky as gelatin and then turned into fluid that means the feathers can be hydrolyzed completely. Keratinolytic protein (Ker) of aforementioned strain was purified using ammonium sulphate precipitation, HiTrap Butyl FF chromatography and Sephacryl S-200 gel filtration. The Ker of P. lilacinus PL-HN-16 had molecular mass of 33 kDa, the optimum pH 8.0 and temperature optimum at 40 degrees C. It used the soluble keratin as substrate. The enzyme showed high activity and stability over a wide range of pH (6.0 to 10.0) and temperature (300C to 600C) values but was completely inhibited by PMSF. Ker of P. lilacinus PL-HN-16 exhibited stability toward SDS. These promising properties make the enzyme a potential candidate for future applications in biotechnological processes as keratin hydrolysis and dehairing during leather processing.
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