Mohanasundaram S et al., (2017) Int. J. Res. Pharm. Sci., 8(3), 282-287 282 ©JK Welfare & Pharmascope Foundation | International Journal of Research in Pharmaceutical Sciences Optimization of production of Extracellular proteolytic keratinase using Streptomyces sp. isolated from poultry plant soil Mohanasundaram S* 1 , Doss VA 2 , Prabhaharan CTA 1 , Joseph J 1 , Venugopal K 1 , Agilandeshwari P 3 , Sudansuhaa C 1 , Balaganesh R 1 , Ramkumar R 1 , Rajaruban MDS 1 , Balaji B 1 1 Department of Biotechnology, Karpaga Vinayaga College of Engineering and Technology, Maduranthagam, Tamil Nadu, India 2 Department of Biochemistry, PSG College of Arts and Science, Coimbatore, Tamil Nadu, India 3 Department of Biotechnology, Vivekananda College of Engineering for Women, Tiruchengode, Tamil Nadu, India ABSTRACT In this study, Proteolytic keratinase was observed from Streptomyces sp., isolated from poultry plant soil and puri- fied by ammonium sulfate fractionation method followed by Gel filtration chromatography. The purified enzyme was further characterized partially which covers the influence of pH, temperature, incubation time, nitrogen sources and metal ions on the activity of proteolytic keratinase. From the results, it was observed that, proteolytic keratinase isolated from the Streptomyces sp. enumerated from the poultry plant soil showed maximal activity at pH 8.0 and at temperature 50oC within 55mins. It was also found that, at the minimum concentration of 2mM BaCl.2H 2 O, CuSO 4 .5H 2 O and MgCl 2 , it showed highest keratinase activity. Keywords: fermentation; Proteolytic keratinase; Streptomyces sp.; stability. INTRODUCTION Wool, bristle, horns, feathers, hoof, etc are some ex- ample waste materials containing huge level of keratin discharged from animal waste, leather and poultry plants (Gousterova et al., 2005). Since these wastes are rich sources of protein and amino acids, they can be utilized as an essential component in animal feed preparations. Few years before, these materials were subjected into high temperature and subsequent mill- ing for some other uses after degradation (Wang and Parson, 1977). Keratin based wastes can be compe- tently degraded by a few bacteria and fungi due to the secretion of keratinolytic peptidases into the culture medium (Onifade et al., 1998). Keratin-like materials cannot be successfully degraded by the peptidases currently included in detergents. Hence, enzyme with high activity has to be finding out to meet the industri- al requirements and for other applications. So far, wide range of microorganisms with proteolytic keratinase activity has been found, including some species of Ba- cillus (Williams et al., 1990), Actinomycetes (Boeckle et al., 1995) and fungi (Santos et al., 1996). Always, there is a constant demand for thermophilic organisms be- cause of their high thermal stability and resistance to- wards denaturation by acidic and alkaline factors. The most important feature of thermophilic organisms is production of enzymes that catalyze biochemical reac- tions at higher levels of temperatures and these en- zymes are widely used in many industrial areas in modern day of science. In recent years, many enzymes from these thermophilic bacteria have been effectively purified, characterized and used in industrial applica- tions (Berna et al., 2015). The aim of this present study is to isolate the Streptomyces species producing extra- cellular proteolytic keratinase from the poultry plant soil and subsequent purification and characterization of the enzyme. MATERIALS AND METHODS Microorganism Streptomyces sp. producing extracellular proteolytic keratinase was isolated from the poultry plant soils from in and around Thirukkalukundram, Kanchipuram district, Tamil Nadu, South India (Dey et al., 1992 and Hinge et al., 1989). Chemicals Solvent and other chemicals which were used in this study were purchased from Himedia, Merck and s.d. Fine-Chemicals, Mumbai, India. Methods Enzyme Production Submerged fermentation was performed by inoculat- ing pure culture of isolate into the production medium www.ijrps.pharmascope.org ISSN: 0975-7538 Research Article * Corresponding Author Email: sbmohan2007@gmail.com Contact: +91-8870903888 Received on: 22-07-2017 Revised on: 29-07-2017 Accepted on: 06-08-2017