Purification and Characterization of Keratinase from Bacillus licheniformis dcs1 for Poultry Waste Processing.

Feather wastes-byproduct of commercial poultry processing plant is produced in large amounts. Keratinolytic enzymes produced by feather degrading bacteria can easily degrade these waste products releasing pure keratin as a residue. The aim of present study was to isolate, and characterize feather degrading bacteria as well as assess the keratinolytic potential of purified enzyme. Three feather degrading bacteria (dps3, wps1 and dcs1) were isolated from feathers of domestic chickens. Preliminary characterization of isolated bacteria revealed these isolates belonging to genus Bacillus. 16S rRNA gene sequencing identified the isolates as B. subtilis dps3 (MW255302), B. cereus wps1 (MW255303) and B. licheniformis dcs1 (MW255304). Cell free supernatant of B. licheniformis dcs1 degraded feathers completely in 14 days indicating its keratinolytic ability. Purification of keratinase enzyme from B. licheniformis dcs1 was performed using column chromatography. SDS-PAGE indicated its molecular weight as 32 KDa. Kerotinolytice activity was maximum at optimum pH of 7 and 45℃ temperature. Enzyme showed the potential to degrade keratin material such as hairs and nails of humans. Findings of current study suggested that purified enzyme possess potential to upgrade nutritional quality of poultry waste containing keratin and might play as important biotechnological tool for keratin hydrolysis.