PhanerochaeteV1, Main, Exploration, bibRecord, 000764

Purification and characteristics of a low-molecular-weight peptide possessing oxidative capacity for phenol from Phanerochaete chrysosporium.

Identifieur interne : 000764 ( Main/Exploration ); précédent : 000763; suivant : 000765

Purification and characteristics of a low-molecular-weight peptide possessing oxidative capacity for phenol from Phanerochaete chrysosporium.

Auteurs : Ming Hu [République populaire de Chine] ; Weican Zhang ; Xuemei Lu ; Peiji Gao

Source :

Science in China. Series C, Life sciences [ 1006-9305 ] ; 2006.

RBID : pubmed:16856493

Descripteurs français

English descriptors

KwdEn :
- Biodegradation, Environmental (MeSH), Chemical Phenomena (MeSH), Chemistry, Physical (MeSH), Fungal Proteins (chemistry), Fungal Proteins (isolation & purification), Fungal Proteins (metabolism), Kinetics (MeSH), Lignin (metabolism), Molecular Weight (MeSH), Monophenol Monooxygenase (chemistry), Monophenol Monooxygenase (isolation & purification), Monophenol Monooxygenase (metabolism), Oxidation-Reduction (MeSH), Peptides (chemistry), Peptides (isolation & purification), Peptides (metabolism), Peroxidases (metabolism), Phanerochaete (metabolism), Phenol (metabolism), Protein Processing, Post-Translational (MeSH), Substrate Specificity (MeSH).
MESH :
- chemical , chemistry : Fungal Proteins, Monophenol Monooxygenase, Peptides.
- chemical , isolation & purification : Fungal Proteins, Monophenol Monooxygenase, Peptides.
- chemical , metabolism : Fungal Proteins, Lignin, Monophenol Monooxygenase, Peptides, Peroxidases, Phenol.
- metabolism : Phanerochaete.
- Biodegradation, Environmental, Chemical Phenomena, Chemistry, Physical, Kinetics, Molecular Weight, Oxidation-Reduction, Protein Processing, Post-Translational, Substrate Specificity.

Abstract

A new low-molecular-weight peptide with phenol oxidase activity, named Pc factor, was isolated and purified from liquid culture of a white-rot basidiomycete Phanerochaete chrysosporium. Its molecular weight was about 600 Da estimated by gel-filtration. Three amino acids Glu, Gly and Val were detected in hydrolysate. Absorption peaks corresponding to amino acids and peptide were observed by UV and IR spectra analysis. And the signal of Ca of amino acid was also detected by 13C-NMR method. Pc factor had high thermostability and remained active in weakly alkalescent pH range. It could chelate Fe3+ and reduce it to Fe2+, but no hydroxyl radical HO* could be detected during the reaction process. It could oxidize phenolic lignin-model compounds such as 2,6-dimethoxyphenol (2,6-DMP), 2,2'-azinobis (3-ethylbenzathiazoline-6-sulfinic acid) (ABTS) and syringaldazine in the absence of Mn2+ and H2O2. These characteristics differed greatly from those of manganese peroxidases. The oxidative catalysis of Pc factor can be enhanced by certain metal ions such as Cu2+ and Mn2+ etc., and O2 molecule was necessary for this reaction. In summary, Pc factor may function as an electron carrier in this novel oxidation-reduction system.

DOI: 10.1007/s11427-006-0243-y
PubMed: 16856493

Affiliations:

République populaire de Chine

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Le document en format XML

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<term>Fungal Proteins (isolation & purification)</term>
<term>Fungal Proteins (metabolism)</term>
<term>Kinetics (MeSH)</term>
<term>Lignin (metabolism)</term>
<term>Molecular Weight (MeSH)</term>
<term>Monophenol Monooxygenase (chemistry)</term>
<term>Monophenol Monooxygenase (isolation & purification)</term>
<term>Monophenol Monooxygenase (metabolism)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Peptides (chemistry)</term>
<term>Peptides (isolation & purification)</term>
<term>Peptides (metabolism)</term>
<term>Peroxidases (metabolism)</term>
<term>Phanerochaete (metabolism)</term>
<term>Phenol (metabolism)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Chimie physique (MeSH)</term>
<term>Cinétique (MeSH)</term>
<term>Dépollution biologique de l'environnement (MeSH)</term>
<term>Lignine (métabolisme)</term>
<term>Masse moléculaire (MeSH)</term>
<term>Maturation post-traductionnelle des protéines (MeSH)</term>
<term>Monophenol monooxygenase (composition chimique)</term>
<term>Monophenol monooxygenase (isolement et purification)</term>
<term>Monophenol monooxygenase (métabolisme)</term>
<term>Oxydoréduction (MeSH)</term>
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<term>Peptides (isolement et purification)</term>
<term>Peptides (métabolisme)</term>
<term>Peroxidases (métabolisme)</term>
<term>Phanerochaete (métabolisme)</term>
<term>Phénol (métabolisme)</term>
<term>Phénomènes chimiques (MeSH)</term>
<term>Protéines fongiques (composition chimique)</term>
<term>Protéines fongiques (isolement et purification)</term>
<term>Protéines fongiques (métabolisme)</term>
<term>Spécificité du substrat (MeSH)</term>
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<term>Monophenol Monooxygenase</term>
<term>Peptides</term>
<term>Peroxidases</term>
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<term>Protéines fongiques</term>
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<term>Dépollution biologique de l'environnement</term>
<term>Masse moléculaire</term>
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<front><div type="abstract" xml:lang="en">A new low-molecular-weight peptide with phenol oxidase activity, named Pc factor, was isolated and purified from liquid culture of a white-rot basidiomycete Phanerochaete chrysosporium. Its molecular weight was about 600 Da estimated by gel-filtration. Three amino acids Glu, Gly and Val were detected in hydrolysate. Absorption peaks corresponding to amino acids and peptide were observed by UV and IR spectra analysis. And the signal of Ca of amino acid was also detected by 13C-NMR method. Pc factor had high thermostability and remained active in weakly alkalescent pH range. It could chelate Fe3+ and reduce it to Fe2+, but no hydroxyl radical HO* could be detected during the reaction process. It could oxidize phenolic lignin-model compounds such as 2,6-dimethoxyphenol (2,6-DMP), 2,2'-azinobis (3-ethylbenzathiazoline-6-sulfinic acid) (ABTS) and syringaldazine in the absence of Mn2+ and H2O2. These characteristics differed greatly from those of manganese peroxidases. The oxidative catalysis of Pc factor can be enhanced by certain metal ions such as Cu2+ and Mn2+ etc., and O2 molecule was necessary for this reaction. In summary, Pc factor may function as an electron carrier in this novel oxidation-reduction system.</div>
</front>
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<ArticleTitle>Purification and characteristics of a low-molecular-weight peptide possessing oxidative capacity for phenol from Phanerochaete chrysosporium.</ArticleTitle>
<Pagination><MedlinePgn>243-50</MedlinePgn>
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<Abstract><AbstractText>A new low-molecular-weight peptide with phenol oxidase activity, named Pc factor, was isolated and purified from liquid culture of a white-rot basidiomycete Phanerochaete chrysosporium. Its molecular weight was about 600 Da estimated by gel-filtration. Three amino acids Glu, Gly and Val were detected in hydrolysate. Absorption peaks corresponding to amino acids and peptide were observed by UV and IR spectra analysis. And the signal of Ca of amino acid was also detected by 13C-NMR method. Pc factor had high thermostability and remained active in weakly alkalescent pH range. It could chelate Fe3+ and reduce it to Fe2+, but no hydroxyl radical HO* could be detected during the reaction process. It could oxidize phenolic lignin-model compounds such as 2,6-dimethoxyphenol (2,6-DMP), 2,2'-azinobis (3-ethylbenzathiazoline-6-sulfinic acid) (ABTS) and syringaldazine in the absence of Mn2+ and H2O2. These characteristics differed greatly from those of manganese peroxidases. The oxidative catalysis of Pc factor can be enhanced by certain metal ions such as Cu2+ and Mn2+ etc., and O2 molecule was necessary for this reaction. In summary, Pc factor may function as an electron carrier in this novel oxidation-reduction system.</AbstractText>
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Purification and characteristics of a low-molecular-weight peptide possessing oxidative capacity for phenol from Phanerochaete chrysosporium.

Purification and characteristics of a low-molecular-weight peptide possessing oxidative capacity for phenol from Phanerochaete chrysosporium.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

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Pour mettre un lien sur cette page dans le réseau Wicri

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