Processing of poultry feathers by alkaline keratin hydrolyzing enzyme from Serratia sp. HPC 1383 |
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| Authors: | Anshuman A. Khardenavis Atya Kapley Hemant J. Purohit |
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| Affiliation: | 1. Department of Biotechnology, Guru Ghasidas Vishwavidyalaya, Bilaspur, Chattisgarh 495009, India;2. School of Biotechnology, Banaras Hindu University, Varanasi, U.P., India;3. Department of Microbiology, Central University of Rajasthan, N.H.8, Bandersindri Kishangarh, Ajmer, India;1. Biotechnology Lab– Bioinovar, Microbiology Institute, Federal University of Rio de Janeiro, Cidade Universitária, 21941-590, Rio de Janeiro, Brazil;2. Embrapa Food Technology, Cereal and Grains Technology and Pilot Plant of Food Extrusion, Guaratiba, 23020-470, Rio de Janeiro, Brazil;3. Embrapa Food Technology Laboratory of Liquid Chromatography, Guaratiba, 23020-470, Rio de Janeiro, Brazil;4. Brazilian Agricultural Research Corporation (EMBRAPA – Headquarters), Biological Station Park, Av. w3 Norte, 70770-901, Brasilia, Brazil;5. Federal Institute of Education, Science, and Technology of Rio de Janeiro, Maracanã, 20270-021, Rio de Janeiro, Brazil;1. Department of Biotechnology, KLE Technological University, Hubballi, Karnataka, 580031, India;2. Department of Biochemistry, Karnatak University, Dharwad, Karnataka, 580003, India;3. Key Laboratory of Urban Pollutant Conversion, Institute of Urban Environment, Chinese Academy of Sciences, Xiamen, China;4. The Department of Chemical, Fibre and Environmental Technology, Federal Institute of Industrial Research Oshodi, Ikeja, Lagos, PMB 21023, Nigeria;1. Laboratório de Bioquímica e Microbiologia Aplicada, Departamento de Ciência de Alimentos (ICTA), Universidade Federal do Rio Grande do Sul, Av. Bento Gonçalves 9500, CEP 91501-970 Porto Alegre, Brazil;2. Laboratório de Ornitologia e Animais Marinhos, Universidade do Vale do Rio dos Sinos, Av. Unisinos 950, CEP 93022-000 São Leopoldo, Brazil;3. Laboratório de Biologia Molecular, Universidade do Vale do Rio dos Sinos, Av. Unisinos 950, CEP 93022-000 São Leopoldo, Brazil |
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| Abstract: | The present study describes the production and characterization of a feather hydrolyzing enzyme by Serratia sp. HPC 1383 isolated from tannery sludge, which was identified by the ability to form clear zones around colonies on milk agar plates. The proteolytic activity was expressed in terms of the micromoles of tyrosine released from substrate casein per ml per min (U/mL min). Induction of the inoculum with protein was essential to stimulate higher activity of the enzyme, with 0.03% feathermeal in the inoculum resulting in increased enzyme activity (45 U/mL) that further increased to 90 U/mL when 3 d old inoculum was used. The highest enzyme activity, 130 U/mL, was observed in the presence of 0.2% yeast extract. The optimum assay temperature and pH for the enzyme were found to be 60 °C and 10.0, respectively. The enzyme had a half-life of 10 min at 60 °C, which improved slightly to 18 min in presence of 1 mM Ca2+. Inhibition of the enzyme by phenylmethyl sulfonyl fluoride (PMSF) indicated that the enzyme was a serine protease. The enzyme was also partially inhibited (39%) by the reducing agent β-mercaptoethanol and by divalent metal ions such as Zn2+ (41% inhibition). However, Ca2+ and Fe2+ resulted in increases in enzyme activity of 15% and 26%, respectively. The kinetic constants of the keratinase were found to be 3.84 μM (Km) and 108.7 μM/mL min (Vmax). These results suggest that this extracellular keratinase may be a useful alternative and eco-friendly route for handling the abundant amount of waste feathers or for applications in other industrial processes. |
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