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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1986 Sep;83(17):6255–6257. doi: 10.1073/pnas.83.17.6255

Peroxidases depolymerize lignin in organic media but not in water

Jonathan S Dordick 1, Michael A Marletta 1, Alexander M Klibanov 1
PMCID: PMC386481  PMID: 16593748

Abstract

Horseradish peroxidase and milk lactoperoxidase, while unable to degrade either synthetic or natural lignins in aqueous solutions, vigorously depolymerize polyconiferyl alcohol, milled wood lignin, and kraft pine lignin in dioxane, dimethylformamide, or methyl formate containing 5% aqueous buffer (10 mM acetate, pH 5). Horseradish peroxidase, solubilized in organic media by chemical modification, can also degrade lignin in native lignocellulose (wheat straw).

Keywords: lignin degradation, biopolymers, enzymes in nonaqueous solvents, ligninase, enzymatic degradation

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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