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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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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Sociedade Brasileira de Microbiologia
2014
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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. |
format | Online Article Text |
id | pubmed-4059287 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Sociedade Brasileira de Microbiologia |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT yehiaramysayed aflatoxindetoxificationbymanganeseperoxidasepurifiedfrompleurotusostreatus |