Abstract

Five pure enzymes (pepsin, trypsin, chymotrypsin, elastase and papain) were used in depilation of goatskins in order to find alternatives to current methods (involving lime and sulphide). The morphologies of depilated skins and hair roots were investigated by both optical microscopy and scanning electron microscopy. There were differences in morphology depending on the possible region of attack of these enzymes at the hair root. Trypsin and elastase were very effective in unhairing with the latter having a generally extensive effect while papain was less so. Pepsin and chymotrypsin were ineffective. The capacity of the enzymes for depilation has also been analyzed in terms of the availability of suitable sites for each of them for cleavage of the various proteins at the hair root and their propensity to cleave has been analyzed through the proteomics tools of the Swiss-Prot program. The results have indicated that theoretical predictions can be correlated to the experimental observations on the depilation of the skin.