ABSTRACT
Advances in microbial enzyme technology offer a significant opportunity for developing low-energy bioconversion solutions for industrial wastes as inexpensive feedstocks for useful products. In this short communication, two agro-food industrial wastes, chicken feather powder (CFP) and okara, were converted into peptides by a Bacillus licheniformis mutant using solid-state fermentation (SSF). The optimum SSF conditions for okara to CFP ratio, inoculum size, and time were 0.7 (7:10), 15%, and 90 h, respectively, which produced 185.99 mg/g peptides, with 910.12 U/g keratinase activity and 85.03% antioxidant scavenging activity. Compared to okara, CFP with mutant strain showed 11.28% higher keratinase activity and produced higher amounts of peptides (5.51%).
Subject(s)
Bacillus licheniformis , Bacillus , Bacillus/genetics , Bacillus licheniformis/genetics , Fermentation , Industrial Waste , PeptidesABSTRACT
Keratinase is one of the important proteases, which is widely used for converting keratin of the keratinaceous materials into various value-added products. In this study, a popular keratinase producer, Bacillus licheniformis PWD-1, was exposed to ultraviolet (UV) and He-Ne laser irradiations to develop high keratinase-producing mutants. Laser irradiation showed a higher lethality of cells (94%) than UV treatment (92%), whereas laser treatment required a longer time (75 min) than UV treatment (20 min). A total of 58 mutants were selected from 176 isolates to study protein and keratinase production capability of the mutants. The highest keratin-to-casein (K:C) ratio (1.43) was exhibited by LU11 mutant, which was obtained from the combined laser and UV irradiations. The purified keratinase (65 kDa) of LU11 showed 40% yield 1.7-fold purity, while the respective value for wild enzyme was 29% and 1.3-fold. Both enzymes showed optimal activity at 55 â and pH 8, with a Z value of 15.78 â for LU11 and 19.72 â for wild strain. The Vmax and specific constant (Kcat/Km) of the mutant enzyme were 357.17 U/ml and 33.11 min-1 mM-1, respectively, which were significantly higher than the respective values of wild enzyme (102.04 U/ml and 28.36 min-1 mM-1).