HAIR REMOVAL POTENTIAL OF KERATINASE PRODUCED BY BACILLUS SPECIES ISOLATED FROM FEATHER WASTE

Abstract

Keratins are tough, fibrous proteins found as the major protein component in hair. Chemical hair removal is harsh and results in severe toxicity and pollution, hence, a need for a non-chemical enzymatic hair removal process. The aim of this study is to characterise keratinase from isolated keratin-degrading Bacillus licheniformis-K51, Bacillus subtilis-K50 and Bacillus sp.-K53 and investigate its potential in hair removal. The collagenolytic ability of keratin-degrading keratinases obtained from Bacillus licheniformis-K51, Bacillus subtilis-K50 and Bacillus sp.-K53 was determined using standard methods. The depilatory potential of keratinase (directly and as part of the constituent of formulated depilatory cream) was determined in vitro on goat skin and in vivo on Wistar rat. Purified keratinases from Bacillus licheniformis-K51 (EZYKer-51), Bacillus subtilis-K50 (EZYKer-50) and Bacillus sp.-K53 (EZYKer-53) did not show significant collagenolytic activities. In vitro treatment of goat skin with EZYKer-51 showed total hair removal within 24 hours and partial hair removal with EZYKer-50 and EZYKer-53. The formulated depilatory cream containing EZYKer-51 showed highest keratinolytic activity (22.20±0.63 U/mL) followed by EZYKer-50 (20.52±0.46 U/mL) and EZYKer-53 (17.06±0.81 U/mL). In vivo depilatory action using formulated cream took 40 min, while that of commercial cream was achieved within 20 min.

Keratinase from Bacillus licheniformis-K51 exhibited complete hair-removal function which makes it potentially suitable in industrial processes involving removal of hair.