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  • Title: Purification and characterization of an efficient poultry feather degrading-protease from Myrothecium verrucaria.
    Author: Moreira-Gasparin FG, de Souza CG, Costa AM, Alexandrino AM, Bracht CK, Boer CG, Peralta RM.
    Journal: Biodegradation; 2009 Sep; 20(5):727-36. PubMed ID: 19381452.
    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 degrees C, with thermal stability at temperatures up to 45 degrees 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 beta-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 beta-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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