Mechanism of enzymatic dehairing of skins using a bacterial alkaline protease.

In the conventional dehairing process of leather manufacture, animal skins are subjected to a drastic chemical treatment using lime and sodium sulfide. Sulfide reduces disulfide bonds in keratin present in hair and epidermis and thereby detaches them from skin. Lime, being an alkali, contributes to opening up of collagen fiber structure by cleaving a major portion of the glycosaminoglycans from proteoglycans, the interfibrillar elements of skin connective tissue. Currently, as an alternative to chemical dehairing, enzyme based dehairing processes using proteases avoiding the use of lime and sulfide are being developed because of their environmental benefits. Though both chemical as well as enzymatic dehairing processes are aimed at removing noncollagenous proteins and proteoglycans in addition to fiber opening, the mechanism of enzymatic process is distinct from that of the chemical process. In this study, we attempt to study in detail the mechanism of hair saving enzymatic dehairing process for skins using a bacterial protease against the customary hair burn chemical dehairing process. Quantitative analysis shows that the collagen content remains unaffected in both treatments but there is a marked reduction of proteoglycan constituents from dehaired pelts in the enzymatic process when compared to lime-sulfide process. This is further substantiated by histochemical examination of the sections of dehaired pelts using different stains as well as immunohistochemical studies on the removal of decorin. HPLC profile shows that decorin is extensively degraded by the bacterial protease. This study conclusively demonstrates that proteolytic degradation of decorin and subsequent removal of proteoglycan aggregates play an important role in the opening up of the collagen fiber bundles during enzymatic dehairing.