PLANT PHYSIOLOGY · 1971 · 20 citations · 13 references
Life SciencesBiochemistryChemistryBiocatalysisCatalysisEnzymologyOxidation ReactionsOxidative Damage To BiomoleculesOxidative Enzymes In FoodsPhenol Oxidase ActivityPhenolic Compound MetabolismPolyphenol Oxidase ActivityPolyphenol OxidasesTwo-dimensional Thin-layer Chromatography
Phloroglucinol and resorcinol are not substrates for clingstone peach (Prunus persica) polyphenol oxidase, but they react with 4-methyl-o-quinone, produced either enzymatically or nonenzymatically, to give an intense red or red-brown color with a maximal absorption at about 470 nanometers. Several colored products were isolated from an ethyl acetate extract of the reaction by two-dimensional thin layer chromatography. Based on thin layer chromatographic and spectral studies of the enzymatic and nonenzymatic reactions, polyphenol oxidase does not play a role in the reaction between 4-methyl-o-quinone and phloroglucinol, resorcinol, d-catechin, or orcinol. In such reactions, the function of polyphenol oxidase is the formation of 4-methyl-o-quinone which then reacts nonenzymatically with the above phenols. Activation energies of both enzymatic and nonenzymatic reactions were determined.
13
Plant phenolic compounds and the isolation of plant enzymes
W.David Loomis, J. Battaile · Phytochemistry · 1966 · 841 citations