Harnessing the Keratinolytic Activity of Bacillus licheniformis Through Random Mutagenesis Using Ultraviolet and Laser Irradiations.

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 ℃ and pH 8, with a Z value of 15.78 ℃ for LU11 and 19.72 ℃ 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).

Bioconversion of agro-food industrial wastes into value-added peptides by a Bacillus sp. Mutant through solid-state fermentation.

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%).