Biochemical characterization of a surfactant-stable keratinase purified from Proteus vulgaris EMB-14 grown on low-cost feather meal
| Autor: | Adeyemi O. Ayodeji, Olufemi S. Bamidele, Michael O. Babalola, Joshua O. Ajele |
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| Rok vydání: | 2020 |
| Předmět: |
0106 biological sciences
0301 basic medicine Proteolysis Proteus vulgaris Bioengineering 01 natural sciences Applied Microbiology and Biotechnology Substrate Specificity Surface-Active Agents 03 medical and health sciences 010608 biotechnology medicine Animals Food science Cell Proliferation biology medicine.diagnostic_test Feather meal Chemistry General Medicine Feathers Hydrogen-Ion Concentration Biodegradation biology.organism_classification Transformation (genetics) 030104 developmental biology Keratinase Sephadex Bioaccumulation biology.protein Keratins Peptide Hydrolases Biotechnology |
| Zdroj: | Biotechnology Letters. 42:2673-2683 |
| ISSN: | 1573-6776 0141-5492 |
| Popis: | The bioaccumulation of keratinous wastes from poultry and dairy industries poses a danger of instability to the biosphere due to resistance to common proteolysis and as such, microbial- and enzyme-mediated biodegradation are discussed. In submerged fermentation medium, Proteus vulgaris EMB-14 utilized and efficiently degraded feather, fur and scales by secreting exogenous keratinase. The keratinase was purified 14-fold as a monomeric 49 kDa by DEAE-Sephadex A-50 anion exchange and Sephadex G-100 size-exclusion chromatography. It exhibited optimum activity at pH 9.0 and 60 °C and was alkaline thermostable (pH 7.0–11.0), retaining 87% of initial activity after 1 h pre-incubation at 60 °C. The Km and Vmax of the keratinase with keratin azure were respectively 0.283 mg/mL and 0.241 U/mL/min. Activity of P. vulgaris keratinase was stimulated by Ca2+, Mg2+, Zn2+, Na+ and maintained in the presence of some denaturing agents, except β-mercaptoethanol while Cu2+ and Pb2+ showed competitive and non-competitive inhibition with Ki 6.5 mM and 17.5 mM, respectively. This purified P. vulgaris keratinase could be surveyed for the biotechnological transformation of bioorganic keratinous wastes into valuable products such as soluble peptides, cosmetics and biodegradable thermoplastics. |
| Databáze: | OpenAIRE |
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