Effective degradation of chicken feather waste by keratinase enzyme with triton X-100 additive

Abstract

Keratinases are a group of proteolytic enzymes which play a crucial role in keratin degradation by breaking the disulfide and peptide bonds of the polypeptide chain of keratin. This study aimed to evaluate the biochemical characteristics of Keratinase enzyme produced from Bacillus licheniformis. The preliminary experimentation was performed in order to find the optimal conditions in which the enzyme showed maximum activity, and also to evaluate its residual activity by using activators and inhibitors. The maximum enzyme yield was 100%, observed at temperature 55 °C and pH 9, and the addition of Triton X-100 markedly enhanced the keratinase activity to 174%. Further on, it was observed that the enzyme activity first increased with the increasing concentrations of Triton-X 100, with maximum residual activity of 184 ± 0.2% at 0.4 (v/v) Triton-X 100 concentration, and then experienced a downfall by further increase in the surfactant concentration, as it came down to 130 ± 0.7% at 0.5 (v/v) concentration of Triton-X 100. The keratinase was finally utilized for the treatment of chicken feathers, and its keratinolytic activity was determined using SEM analysis.