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Conventional leather processing involving depilation of animal hide by lime and sulphide treatment generates considerable amounts of chemical waste causing severe environmental pollution. Enzymatic depilation is an environmentally friendly process and has been considered to be a viable alternative to the chemical depilation process. We isolated an extracellular protease from  Pseudomonas aeruginosa  strain MCM B-327 with high depilation activity using buffalo hide as a substrate. This 33 kDa protease generated a peptide mass fingerprint and  de novo  sequence that matched perfectly with LasB (elastase), of  Pseudomonas aeruginosa . In support of this data a  lasB  mutant of MCM B-327 strain lacked depilatory activity and failed to produce LasB. LasB heterologously over-produced and purified from  Escherichia coli  also exhibited high depilating activity. Moreover, reintroduction of the  lasB  gene to the  P. aeruginosa lasB  mutant  via  a knock-in strategy also successfully restored depilation activity thus confirming the role of LasB as the depilating enzyme.

Enzymatic Depilation of Animal Hide: Identification of Elastase (LasB) from Pseudomonas aeruginosa MCM B-327 as a Depilating Protease