Production and characterization of keratinase by Ochrobactrum intermedium for feather keratin utilization

A newly isolated bacterium producing 55.5 U/mL keratinase on feather meal minimal medium was identified as Ochrobactrum intermedium . Optimization of process parameters by one-variable-at-a-time (OVAT) approach (substrate concentration 0.5% w/v, inoculum size 5% w/v, pH 7.0, 200 rpm for 96 h at 40 °C) resulted in 2.1-fold increase in keratinase secretion (117 U/mL). Keratinase was optimally active at pH 9.0 and 40 °C and was stable at pH 9.0 and 60 °C for 120 min. Calcium ions enhanced keratinase activity (158%) significantly, while it was strongly inhibited by both PMSF and EDTA, indicating it to be a metallo-serine protease. Keratinase degraded native chicken feathers efficiently resulting in 97.9% weight loss along with release of 745.5 μg/mL soluble proteins and 4196.69 μg/mL amino acids. Feather hydrolysate generated by NKIS 1 exhibited significant anti-oxidant and free-radical scavenging activity (90.46%). The present study revealed that O. intermedium NKIS 1 has potential applications in the biodegradation of chicken feathers and the value-addition of poultry waste. • Ochrobactrum intermedium NKIS 1 produced 55.5 U ml −1 keratinase on feather meal. • Optimization resulted in 2.1-fold increased keratinase secretion (117 U ml −1 ). • It was optimally active at pH 9.0 and 40 °C and stable at pH 9.0 and 60 °C. • Its activity was significantly stimulated in presence of Calcium ions (158%). • The said strain resulted in 97.9% of native chicken feathers biodegradation.