Characterization of manganese-dependent peroxidase isoenzymes from the ligninolytic fungus Phanerochaete flavido-alba.
Identifieur interne : 000979 ( Main/Curation ); précédent : 000978; suivant : 000980Characterization of manganese-dependent peroxidase isoenzymes from the ligninolytic fungus Phanerochaete flavido-alba.
Auteurs : Teresa De La Rubia [Espagne] ; Araceli Linares ; Juana Pérez ; José Mu Oz-Dorado ; José Romera ; José MartínezSource :
- Research in microbiology [ 0923-2508 ] ; 2002.
Descripteurs français
- KwdFr :
- Cinétique (MeSH), Données de séquences moléculaires (MeSH), Dépollution biologique de l'environnement (MeSH), Huile d'olive (MeSH), Huiles végétales (MeSH), Isoenzymes (génétique), Isoenzymes (isolement et purification), Isoenzymes (métabolisme), Lignine (métabolisme), Manganèse (MeSH), Peroxidases (génétique), Peroxidases (isolement et purification), Peroxidases (métabolisme), Phanerochaete (croissance et développement), Phanerochaete (enzymologie), Phanerochaete (génétique), Polluants de l'eau (pharmacologie), Similitude de séquences d'acides aminés (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- croissance et développement : Phanerochaete.
- enzymologie : Phanerochaete.
- génétique : Isoenzymes, Peroxidases, Phanerochaete.
- isolement et purification : Isoenzymes, Peroxidases.
- métabolisme : Isoenzymes, Lignine, Peroxidases.
- pharmacologie : Polluants de l'eau.
- Cinétique, Données de séquences moléculaires, Dépollution biologique de l'environnement, Huile d'olive, Huiles végétales, Manganèse, Similitude de séquences d'acides aminés, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Biodegradation, Environmental (MeSH), Isoenzymes (genetics), Isoenzymes (isolation & purification), Isoenzymes (metabolism), Kinetics (MeSH), Lignin (metabolism), Manganese (MeSH), Molecular Sequence Data (MeSH), Olive Oil (MeSH), Peroxidases (genetics), Peroxidases (isolation & purification), Peroxidases (metabolism), Phanerochaete (enzymology), Phanerochaete (genetics), Phanerochaete (growth & development), Plant Oils (MeSH), Sequence Homology, Amino Acid (MeSH), Water Pollutants (pharmacology).
- MESH :
- chemical , genetics : Isoenzymes, Peroxidases.
- chemical , isolation & purification : Isoenzymes, Peroxidases.
- chemical , metabolism : Isoenzymes, Lignin, Peroxidases.
- enzymology : Phanerochaete.
- genetics : Phanerochaete.
- growth & development : Phanerochaete.
- chemical , pharmacology : Water Pollutants.
- Amino Acid Sequence, Biodegradation, Environmental, Kinetics, Manganese, Molecular Sequence Data, Olive Oil, Plant Oils, Sequence Homology, Amino Acid.
Abstract
Phanerochaete flavido-alba is able to decolorize and detoxify olive oil wastewater (OMW) in a process in which simple and polymeric phenols are removed. An unusual acidic MnP is accumulated during the degradation course. This microorganism produces two families of MnPs. MnP1 has an apparent molecular weight of 45 kDa and is secreted as a mixture of isoenzymes with pI ranging from 5.6 to 4.75. MnP2, which is produced as an unique isoenzyme, has an apparent molecular weight of 55.6 Mr and an unusual acidic pI lower than 2.8. The higher specific peroxidase activity for purified MnP2 was for Mn2+ oxidation. Hydroquinone and methylhydroquinone oxidation by MnP2 was Mn2+ dependent, in reaction mixtures without exogenous H2O2. Conversely, ABTS oxidation was Mn2+ independent. Two different DNA fragments (mnpA and mnpB), amplified by PCR, using MnP2 N-terminal sequence and oligonucleotides deduced from two conserved sequences of other MnPs, code for MnPs that belong to the P. chrysosporium mnp2 subfamily on the basis of intron position. The structure of mnpA and mnpB seems to be related to known manganese peroxidase genes, but mnpA encodes an Alanine instead of a Serine (Ser168) regarded as invariant within typical MnPs.
DOI: 10.1016/s0923-2508(02)01357-8
PubMed: 12437216
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pubmed:12437216Le document en format XML
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<term>Peroxidases (isolation & purification)</term>
<term>Peroxidases (metabolism)</term>
<term>Phanerochaete (enzymology)</term>
<term>Phanerochaete (genetics)</term>
<term>Phanerochaete (growth & development)</term>
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<term>Sequence Homology, Amino Acid (MeSH)</term>
<term>Water Pollutants (pharmacology)</term>
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<term>Données de séquences moléculaires (MeSH)</term>
<term>Dépollution biologique de l'environnement (MeSH)</term>
<term>Huile d'olive (MeSH)</term>
<term>Huiles végétales (MeSH)</term>
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<term>Isoenzymes (isolement et purification)</term>
<term>Isoenzymes (métabolisme)</term>
<term>Lignine (métabolisme)</term>
<term>Manganèse (MeSH)</term>
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<term>Molecular Sequence Data</term>
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<term>Huiles végétales</term>
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<front><div type="abstract" xml:lang="en">Phanerochaete flavido-alba is able to decolorize and detoxify olive oil wastewater (OMW) in a process in which simple and polymeric phenols are removed. An unusual acidic MnP is accumulated during the degradation course. This microorganism produces two families of MnPs. MnP1 has an apparent molecular weight of 45 kDa and is secreted as a mixture of isoenzymes with pI ranging from 5.6 to 4.75. MnP2, which is produced as an unique isoenzyme, has an apparent molecular weight of 55.6 Mr and an unusual acidic pI lower than 2.8. The higher specific peroxidase activity for purified MnP2 was for Mn2+ oxidation. Hydroquinone and methylhydroquinone oxidation by MnP2 was Mn2+ dependent, in reaction mixtures without exogenous H2O2. Conversely, ABTS oxidation was Mn2+ independent. Two different DNA fragments (mnpA and mnpB), amplified by PCR, using MnP2 N-terminal sequence and oligonucleotides deduced from two conserved sequences of other MnPs, code for MnPs that belong to the P. chrysosporium mnp2 subfamily on the basis of intron position. The structure of mnpA and mnpB seems to be related to known manganese peroxidase genes, but mnpA encodes an Alanine instead of a Serine (Ser168) regarded as invariant within typical MnPs.</div>
</front>
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<Abstract><AbstractText>Phanerochaete flavido-alba is able to decolorize and detoxify olive oil wastewater (OMW) in a process in which simple and polymeric phenols are removed. An unusual acidic MnP is accumulated during the degradation course. This microorganism produces two families of MnPs. MnP1 has an apparent molecular weight of 45 kDa and is secreted as a mixture of isoenzymes with pI ranging from 5.6 to 4.75. MnP2, which is produced as an unique isoenzyme, has an apparent molecular weight of 55.6 Mr and an unusual acidic pI lower than 2.8. The higher specific peroxidase activity for purified MnP2 was for Mn2+ oxidation. Hydroquinone and methylhydroquinone oxidation by MnP2 was Mn2+ dependent, in reaction mixtures without exogenous H2O2. Conversely, ABTS oxidation was Mn2+ independent. Two different DNA fragments (mnpA and mnpB), amplified by PCR, using MnP2 N-terminal sequence and oligonucleotides deduced from two conserved sequences of other MnPs, code for MnPs that belong to the P. chrysosporium mnp2 subfamily on the basis of intron position. The structure of mnpA and mnpB seems to be related to known manganese peroxidase genes, but mnpA encodes an Alanine instead of a Serine (Ser168) regarded as invariant within typical MnPs.</AbstractText>
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