Abstract
Horseradish peroxidase displayed a ping-pong kinetic reaction mechanism with lignin model compounds and lignins. Oxidation of the α carbon on acetosyringone or acetovanillone failed above pH 6.5, while conversion of α-methylsyringyl (or guaiacyl) alcohol to acetosyringone (or vanillone) occurred optimally at pH 7.8. Small MW fragments were not formed from lignins at pH 6.4 and 7.8. These observations provide evidence for the growing concept that freely soluble peroxidase is not a lignolytic enzyme.
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