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http://dx.doi.org/10.12989/aer.2022.11.1.001

Metallo-collagenase production by Arthrobacter creatinolyticus KP015744  

Savita A. Kate (Department of Biotechnology, Shivchhatrapati College)
Madhuri Sahasrabudhe (Department of Microbiology Maulana Azad College of Arts, Science and Commerce)
Archana Pethe (Department of Microbiology, Shivaji College of Arts, Commerce and Science)
Publication Information
Advances in environmental research / v.11, no.1, 2022 , pp. 1-16 More about this Journal
Abstract
Amongst 27 isolates from deteriorated leather samples, Arthrobacter creatinolyticus KP015744 zzx28 was found to be an efficient collagenase producer. Collagenase production of 13.33 µmoles/min was shown at an optimum temperature at 37℃ after 72h and at pH 7.5 by using 2 ml/dL inoculum in 10 mg/ml collagen peptide type I as a substrate. In presence of Hg2+, EDTA and 𝛽-mercaptoethanol the collagenase production by the isolate was strongly inhibited however Fe2+, Ca2+and DMSO enhanced production of the enzyme. Specific activity was found to be 19.46×103 U/mg and molecular weight 66 kD by SDS PAGE. Isolate also has potential to hydrolyze keratin which is another important protein found in leather. Experimental results propose that collagenase can be effectively used as a tool for collagen and keratin rich solid waste treatment.
Keywords
collagen peptide type I; dialysis; EDTA; feather meal; leather; metalloprotease;
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