Purification and characterization of an efficient poultry feather degrading-protease from Myrothecium verrucaria |
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Authors: | Fabiana G Moreira-Gasparin Cristina G Marques de Souza Andréa M Costa Ana Maria Alexandrino Cissa K Bracht Cinthia G Boer Rosane M Peralta |
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Institution: | (1) Departamento de Bioquímica, Universidade Estadual de Maringá, Av. Colombo, 5790, Maringá, PR, 87020-900, Brazil |
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Abstract: | The purpose of this work was to characterize an alkaline protease from the filamentous fungus Myrothecium verrucaria and to explore its capability to degrade native poultry feathers. The enzyme was purified to homogeneity using a single chromatographic
step. Recovery was high, 62%, with a specific activity of 12,851.8 U/mg protein. The enzyme is a small monomeric protein with
a molecular mass of 22 ± 1.5 kDa. It presented pH optimum of 8.3 and was stable over a broad pH range (5.0–12.0). The temperature
optimum was 37°C, with thermal stability at temperatures up to 45°C. The enzyme presented an efficiency of 80.3% in the degradation
of poultry feather meal, releasing amino acids and soluble peptides. It was able to hydrolyze β-keratin without necessity of chemical or enzymatic reduction of the disulphide bonds. Considering that, everyday, poultry-processing
plants produce feathers as a waste products, this protease can be useful in biotechnological processes aiming to improve the
transformation of poultry feathers through solubilization of β-keratin into usable peptides. Furthermore, it can also be useful in processes aiming to reduce the environmental pollution
caused by the accumulation of feathers. |
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Keywords: | Biodegradation Keratinase Poultry feather Protein purification Submerged cultures |
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