In vitro degradation of insoluble lignin in aqueous media by lignin peroxidase and manganese peroxidase.
Identifieur interne : 000B72 ( Main/Exploration ); précédent : 000B71; suivant : 000B73In vitro degradation of insoluble lignin in aqueous media by lignin peroxidase and manganese peroxidase.
Auteurs : D N Thompson [États-Unis] ; B R Hames ; C A Reddy ; H E GrethleinSource :
- Applied biochemistry and biotechnology [ 0273-2289 ] ; 1998.
Abstract
The abilities of lignin peroxidase (LIP) and manganese peroxidase (MNP) from Phanerochaete chrysosporium to degrade an insoluble hardwood lignin in vitro in aqueous media were tested. Neither LIP nor MNP appreciably changed the mass or lignin content, although both produced small amounts of unique solubilized lignin fragments. Treatment with both LIP and MNP, however, decreased the mass by 11%, decreased the lignin content by 5.1% (4.2% as total weight), and solubilized unique lignin-derived molecules. These results suggest that LIP and MNP synergistically degrade high molecular weight insoluble lignin, but singly, neither enzyme is sufficient to effect lignin degradation.
DOI: 10.1007/BF02920207
PubMed: 18576060
Affiliations:
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Le document en format XML
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<front><div type="abstract" xml:lang="en">The abilities of lignin peroxidase (LIP) and manganese peroxidase (MNP) from Phanerochaete chrysosporium to degrade an insoluble hardwood lignin in vitro in aqueous media were tested. Neither LIP nor MNP appreciably changed the mass or lignin content, although both produced small amounts of unique solubilized lignin fragments. Treatment with both LIP and MNP, however, decreased the mass by 11%, decreased the lignin content by 5.1% (4.2% as total weight), and solubilized unique lignin-derived molecules. These results suggest that LIP and MNP synergistically degrade high molecular weight insoluble lignin, but singly, neither enzyme is sufficient to effect lignin degradation.</div>
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