New Bacillus paralicheniformis strain with high proteolytic and keratinolytic activity
S. Aktayeva, Bekbolat Khassenov
Abstract
Abstract Bacillus paralicheniformis T7, which exhibits high proteolytic and keratinolytic activities, was isolated from soil in Kazakhstan. Its secreted proteases were thermostable and alkaline, demonstrating maximum activity at 70 °C and pH 9.0. The proteases and keratinases of this strain were sensitive to Ni 2+ , Co 2+ , Mn 2+ , and Cd 2+ , with Cu 2+ , Co 2+ and Cd 2+ negatively affecting keratinolytic activity, and Fe 3+ ions have a strong inhibitory effect on proteolytic and keratinolytic activity. Seven proteases were identified in the enzymatic extract of B . paralicheniformis T7: four from the serine peptidase family and three from the metallopeptidase family. The proteases hydrolyzed 1 mg of casein, hemoglobin, gelatin, ovalbumin, bovine serum albumin, or keratin within 15 s to 30 min. The high keratinolytic activity of this strain was confirmed through the degradation of chicken feathers, horns, hooves, wool, and cattle hide. Chicken feathers were hydrolyzed in 4 days, and the degrees of hydrolysis for cattle hide, wool, hoof, and horn after 7 days of cultivation were 97.2, 34.5, 29.6, and 3.6%, respectively. During submerged fermentation with feather medium in a laboratory bioreactor, the strain secreted enzymes with 249.20 ± 7.88 U/mL protease activity after 24 h. Thus, B. paralicheniformis T7 can be used to produce proteolytic and keratinolytic enzymes for application in processing proteinaceous raw materials and keratinous animal waste.