You are not currently logged in.
Access your personal account or get JSTOR access through your library or other institution:
If You Use a Screen ReaderThis content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Peroxidases Depolymerize Lignin in Organic Media but not in Water
Jonathan S. Dordick, Michael A. Marletta and Alexander M. Klibanov
Proceedings of the National Academy of Sciences of the United States of America
Vol. 83, No. 17 (Sep. 1, 1986), pp. 6255-6257
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/28335
Page Count: 3
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Preview not available
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).
Proceedings of the National Academy of Sciences of the United States of America © 1986 National Academy of Sciences