Bacillus sp is microorganism’s species which can produce keratinase en-zyme. The enzyme has ability to degrade keratine substrate and it belongs to extracellular inducible enzyme group. In this study, proteolitic activities of Bacillus strains isolated from soil contaminated with poultry farm waste were determined on Skim milk Agar. 63 Bacillus strains were identified as proteolytic. Nine of these strains showed activity with the keratin-azure substrate and were determined to be keratinolytic. Among the isolated strains, strain no: 30 was selected as the best keratinase producer. The ba-sal feather medium was used to produce keratinase. The optimum produc-tion conditions of the enzyme were determined as pH = 8.0 and 30℃. The optimum activity of the enzyme was determined at pH: 9.0 and 50℃. When the enzyme was pre-incubated for 30 minutes at 50℃ - 100℃, it preserved its activity at a high rate (90%) after pre-incubation at 50℃ and showed no activity after pre-incubations above 70 degrees. After 30 minutes of pre-incubation of the enzyme with 1 - 5 mM concentrations of chemical and metal ions, it was determined that tween 20 (215%) and SDS (204%) significantly increased the activity, and EDTA (76%), Urea (40%), ZnCl2 (28%), MgCl2 (51%), NiCl2 (24%), CaCl2 (56%), HgCl2 (0), CuCl2 (83%) decreased the activity.
Cite this paper
Dansoko, A. S. (2024). Production and Characterization of Keratinase Enzyme from Natural Isolate Bacillus Strains. Open Access Library Journal, 11, e1184. doi: http://dx.doi.org/10.4236/oalib.1111184.
Singh, R., Singh, T. and Pandey, A. (2019) Microbial Enzymes—An Overview. In Biomass, Biofuels, Biochemicals: Advances in Enzyme Technology, Elsevier E.V., Netherlands, 1-40. https://doi.org/10.1016/B978-0-444-64114-4.00001-7
Dey, A. and Bhunia, B. (2019) Recent Advances in Strain Improvement, Production, Purification and Applications of Industrial Enzyme. Recent Patents on Biotechnology, 13, 3. https://doi.org/10.2174/187220831301190201122202
Syed, U. and Yona, G. (2009) Enzyme Function Prediction with Interpretable Models. Methods in Molecular Biology, 541, 373-420. https://doi.org/10.1007/978-1-59745-243-4_17
Nagal, S. and Jain, P.C. (2010) Feather Degradation by Strains of Bacillus Isolated from Decomposing Feathers. Brazilian Journal of Microbiology, 41, 196-200.
Arokiyaraj, S., et al. (2019) Optimizing the Fermentation Conditions and Enhanced Production of Keratinase from Bacillus cereus Isolated from Halophilic Environment. Saudi Journal of Biological Sciences, 26, 378-381. https://doi.org/10.1016/j.sjbs.2018.10.011
Gonzalo, M., et al. (2020) Azo Dying of α-Keratin Material Improves Microbial Keratinase Screening and Standardization. Microbial Biotechnology, 13, 984-996. https://doi.org/10.1111/1751-7915.13541
Tamreihao, K. (2018) Feather Degradation by Keratinolytic Bacteria and Biofertilizing Potential for Sustainable Agricultural Production. Journal of Basic Microbiology, 59, 4-13. https://doi.org/10.1002/jobm.201800434
Hamiche, S., Mechri, S., Khelouia, L., Annane, A., El Hattab, M., Badis, A. and Jaouadi, B. (2019) Purification and Biochemical Characterization of Two Keratinases from Bacillus amyloliquefaciens S13 Iso-lated from Marine Brown Alga Zonaria tournefortii with Potential Keratin-Biodegradation and Hideunhairing Activities. Interna-tional Journal of Biological Macromolecules, 122, 758-769. https://doi.org/10.1016/j.ijbiomac.2018.10.174
Singh, R.S., Singh, T. and Pandey, A. (2019) Thermostable and Halotolerant Keratinase from Bacillus aerius NSMk2 with Remarkable Dehairing and Laundary Applications. Journal of Basic Microbiology, 2019, 40.
Saraiva, J.A., Claudia, C.S., Nunes, S. and Coimbra, M.A. (2010) Purification and Characterization of Olive (Olea europaea L.) Peroxidases. Departamento de Química, Universidade de Aveiro, Campus Universitário de Santiago, Aveiro, Portugal.
Yusuf, I., et al. (2015) Investigation of Keratinase Activity and Feather Degradation Ability of Immobilised Bacillus sp. Khayat in the Presence of Heavy Metals in a Semi Continuous Fermentation.
