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Methylene blue as a lignin surrogate in manganese peroxidase reaction systems.

Identifieur interne : 000160 ( Main/Exploration ); précédent : 000159; suivant : 000161

Methylene blue as a lignin surrogate in manganese peroxidase reaction systems.

Auteurs : Jeffrey D. Goby [États-Unis] ; Michael H. Penner [États-Unis] ; Curtis A. Lajoie [États-Unis] ; Christine J. Kelly [États-Unis]

Source :

RBID : pubmed:28823615

Descripteurs français

English descriptors

Abstract

Manganese peroxidase (MnP) is associated with lignin degradation and is thus relevant to lignocellulosic-utilization technologies. Technological applications require reaction mixture optimization. A surrogate substrate can facilitate this if its susceptibility to degradation is easily monitored and mirrors that of lignin. The dye methylene blue (MB) was evaluated in these respects as a surrogate substrate by testing its reactivity in reaction mixtures containing relevant redox mediators (dicarboxylic acids, fatty acids). Relative rates of MB degradation were compared to available literature reports of lignin degradation under similar conditions, and suggest that MB can be a useful lignin surrogate in MnP systems.

DOI: 10.1016/j.ab.2017.08.010
PubMed: 28823615


Affiliations:


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Le document en format XML

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<term>Fatty Acids, Unsaturated (chemistry)</term>
<term>Lignin (chemistry)</term>
<term>Lignin (metabolism)</term>
<term>Methylene Blue (chemistry)</term>
<term>Methylene Blue (metabolism)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Peroxidases (genetics)</term>
<term>Peroxidases (metabolism)</term>
<term>Phanerochaete (enzymology)</term>
<term>Recombinant Proteins (genetics)</term>
<term>Recombinant Proteins (metabolism)</term>
<term>Spectrophotometry (MeSH)</term>
<term>Substrate Specificity (MeSH)</term>
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<term>Acides gras insaturés (composition chimique)</term>
<term>Bleu de méthylène (composition chimique)</term>
<term>Bleu de méthylène (métabolisme)</term>
<term>Lignine (composition chimique)</term>
<term>Lignine (métabolisme)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Peroxidases (génétique)</term>
<term>Peroxidases (métabolisme)</term>
<term>Phanerochaete (enzymologie)</term>
<term>Protéines recombinantes (génétique)</term>
<term>Protéines recombinantes (métabolisme)</term>
<term>Spectrophotométrie (MeSH)</term>
<term>Spécificité du substrat (MeSH)</term>
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<term>Fatty Acids, Unsaturated</term>
<term>Lignin</term>
<term>Methylene Blue</term>
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<term>Peroxidases</term>
<term>Recombinant Proteins</term>
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<term>Methylene Blue</term>
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<term>Recombinant Proteins</term>
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<term>Acides gras insaturés</term>
<term>Bleu de méthylène</term>
<term>Lignine</term>
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<term>Phanerochaete</term>
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<term>Lignine</term>
<term>Peroxidases</term>
<term>Protéines recombinantes</term>
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<term>Spectrophotometry</term>
<term>Substrate Specificity</term>
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<term>Spectrophotométrie</term>
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<div type="abstract" xml:lang="en">Manganese peroxidase (MnP) is associated with lignin degradation and is thus relevant to lignocellulosic-utilization technologies. Technological applications require reaction mixture optimization. A surrogate substrate can facilitate this if its susceptibility to degradation is easily monitored and mirrors that of lignin. The dye methylene blue (MB) was evaluated in these respects as a surrogate substrate by testing its reactivity in reaction mixtures containing relevant redox mediators (dicarboxylic acids, fatty acids). Relative rates of MB degradation were compared to available literature reports of lignin degradation under similar conditions, and suggest that MB can be a useful lignin surrogate in MnP systems.</div>
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