Characterization of betacyanin oxidation catalyzed by a peroxidase from Beta vulgaris L. roots

A protein fraction with peroxidase (EC 1.11.1.7) activity against guaiacol from Beta vulgaris L. roots oxidized both betanidin and betanin (betanidin 5-O-beta -D-glucoside), the former being the more efficient substrate for t he enzyme. The protein fraction contained three strongly basic perxidase is oenzymes. Betanidin quinone was formed as the only product in the course of enzymatic betanidin oxidation, whereas betalamic acid and several oxidized cyclo-DOPA 5-O-beta -D-glucoside polymers were generated during the oxidat ion of betanin. In accordance with the catalytic properties of peroxidase, a possible mechanism for betanidin oxidation is proposed. This mechanism in cludes the formation of a betanidin radical, which, by further dismutation, yields betanidin quinone and betanidin. The betanidin oxidation rate showe d a Michaelis-type dependence on the substrate concentration. The apparent K-M for the reaction was 0.46 mM. On the basis of the spectral properties o f the enzyme responsible for both betanidin and betanin oxidations, its per oxidase nature is suggested.