Abstract
Collagenase production by Penicillium sp. isolated from deteriorated leather sample was studied. The isolate produced collagenase 802.43±15.81U/ml at optimum temperature 30ºC and at pH 6.5 within 5 days using 1% collagen peptide type I as a substrate. Ca++ ions were found to be the best activator whereas EDTA and β-mercaptoethanol inhibited collagenase production. The isolate was also found to produce caseinase, gelatinase and keratinase. Experimental results propose that the isolate having ability to produce broad range of enzymes can be effectively used as a tool for leather industry waste treatment.
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