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Aflatoxin detoxification by manganese peroxidase purified from Pleurotus ostreatus

Manganese peroxidase (MnP) was produced from white rot edible mushroom Pleurotus ostreatus on the culture filtrate. The enzyme was purified to homogeneity using (NH(4))(2)SO(4) precipitation, DEAE-Sepharose and Sephadex G-100 column chromatography. The final enzyme activity achieved 81 U mL(−1), spe...

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Autor principal: Yehia, Ramy Sayed
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Sociedade Brasileira de Microbiologia 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4059287/
https://www.ncbi.nlm.nih.gov/pubmed/24948923
http://dx.doi.org/10.1590/S1517-83822014005000026
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author Yehia, Ramy Sayed
author_facet Yehia, Ramy Sayed
author_sort Yehia, Ramy Sayed
collection PubMed
description Manganese peroxidase (MnP) was produced from white rot edible mushroom Pleurotus ostreatus on the culture filtrate. The enzyme was purified to homogeneity using (NH(4))(2)SO(4) precipitation, DEAE-Sepharose and Sephadex G-100 column chromatography. The final enzyme activity achieved 81 U mL(−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 °C. The pure MnP activity was enhanced by Mn(2+), Cu(2+), Ca(2+) and K(+) and inhibited by Hg(+2) and Cd(+2). H(2)O(2) at 5 mM enhanced MnP activity while at 10 mM inhibited it significantly. The MnP-cDNA encoding gene was sequenced and determined (GenBank accession no. AB698450.1). The MnP-cDNA was found to consist of 497 bp in an Open Reading Frame (ORF) encoding 165 amino acids. MnP from P. ostreatus could detoxify aflatoxin B1 (AFB1) depending on enzyme concentration and incubation period. The highest detoxification power (90%) was observed after 48 h incubation at 1.5 U mL(−1) enzyme activities.
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spelling pubmed-40592872014-06-19 Aflatoxin detoxification by manganese peroxidase purified from Pleurotus ostreatus Yehia, Ramy Sayed Braz J Microbiol Research Paper Manganese peroxidase (MnP) was produced from white rot edible mushroom Pleurotus ostreatus on the culture filtrate. The enzyme was purified to homogeneity using (NH(4))(2)SO(4) precipitation, DEAE-Sepharose and Sephadex G-100 column chromatography. The final enzyme activity achieved 81 U mL(−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 °C. The pure MnP activity was enhanced by Mn(2+), Cu(2+), Ca(2+) and K(+) and inhibited by Hg(+2) and Cd(+2). H(2)O(2) at 5 mM enhanced MnP activity while at 10 mM inhibited it significantly. The MnP-cDNA encoding gene was sequenced and determined (GenBank accession no. AB698450.1). The MnP-cDNA was found to consist of 497 bp in an Open Reading Frame (ORF) encoding 165 amino acids. MnP from P. ostreatus could detoxify aflatoxin B1 (AFB1) depending on enzyme concentration and incubation period. The highest detoxification power (90%) was observed after 48 h incubation at 1.5 U mL(−1) enzyme activities. Sociedade Brasileira de Microbiologia 2014-05-19 /pmc/articles/PMC4059287/ /pubmed/24948923 http://dx.doi.org/10.1590/S1517-83822014005000026 Text en Copyright © 2014, Sociedade Brasileira de Microbiologia All the content of the journal, except where otherwise noted, is licensed under a Creative Commons License CC BY-NC.
spellingShingle Research Paper
Yehia, Ramy Sayed
Aflatoxin detoxification by manganese peroxidase purified from Pleurotus ostreatus
title Aflatoxin detoxification by manganese peroxidase purified from Pleurotus ostreatus
title_full Aflatoxin detoxification by manganese peroxidase purified from Pleurotus ostreatus
title_fullStr Aflatoxin detoxification by manganese peroxidase purified from Pleurotus ostreatus
title_full_unstemmed Aflatoxin detoxification by manganese peroxidase purified from Pleurotus ostreatus
title_short Aflatoxin detoxification by manganese peroxidase purified from Pleurotus ostreatus
title_sort aflatoxin detoxification by manganese peroxidase purified from pleurotus ostreatus
topic Research Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4059287/
https://www.ncbi.nlm.nih.gov/pubmed/24948923
http://dx.doi.org/10.1590/S1517-83822014005000026
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