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Aflatoxin detoxification by manganese peroxidase purified from Pleurotus ostreatus BJM
Yehia,Ramy Sayed.
Manganese peroxidase (MnP) was produced from white rot edible mushroom Pleurotus ostreatus on the culture filtrate. The enzyme was purified to homogeneity using (NH4)2SO4 precipitation, DEAE-Sepharose and Sephadex G-100 column chromatography. The final enzyme activity achieved 81UmL-1, specific activity 78 U mg-1 with purification fold of 130 and recovery 1.2% of the crude enzyme. SDS-PAGE indicated that the pure enzyme have a molecular mass of approximately 42 kDa. The optimum pH was between 4-5 and the optimum temperature was 25 ºC. The pure MnP activity was enhanced by Mn2+,Cu2+,Ca2+ and K+ and inhibited by Hg+2 and Cd+2.H2O2 at 5 mM enhanced MnP activity while at 10 mM inhibited it significantly. The MnP-cDNA encoding gene was sequenced and determined...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Manganese peroxidase; Aflatoxin B1; Pleurotus ostreatus; Purification.
Ano: 2014 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822014000100018
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