Screening and Isolation of Collagenase Producing Microorganism from Proteins Waste Found in Himalayan Region

Document Type : Original Article


Department of Biotechnology, Himachal Pradesh University, Summer Hill, Shimla, India


Multicellular organisms of the human and animal bodies such as skin, bones, tendons, cartilage and blood vessels have collagen as a fibrous element. Collagen is a most representative protein of the leather wastes and collagenase is a proteolytic enzyme. The collagenase is responsible for the degradation of native collagen to small peptide fragments, without affecting the other proteins. Collagenase has widespread applications such as cosmetics, wound healing, diabetic ulcer, arterial ulcers and burns surgery, etc. In the present study, Twenty-seven collagenase-producing microorganisms were identified and isolated from soil/sewage samples of the fish market and slaughterhouse areas. CS-20 sample was found most efficient producer microorganism of collagenase. This sample was identified from Pseudomonas genus and isolated as Pseudomonas species. The parameters such as temperature, substrate, pH, incubation period and inoculum percentage were also optimized to screen the hyper producer strain with maximum collagenase activity. CS-20 isolate (Collagenase producing microorganism) was capable of hydrolyzing other protein substrates such as gelatine and azocoll. Thus, CS-20 isolate is high-efficiency strain for the production of collagenase.


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