Abstract
Gallic acid, pyrogallol and gallic acid methyl ester were kinetically characterised as substrates of polyphenoloxidase (PPO) and peroxidase (POD) and their pro- and anti-oxidant capacities were studied. The data obtained are correlated with the chemical shifts of the carbons supporting the vicinal hydroxyls obtained by 13C NMR. Pyrogallol showed the highest catalytic constant for both PPO and POD, reflecting its low δ 2 value. This also implies that both enzymes have a high Michaelis constant for pyrogallol. Pyrogallol also showed higher pro- and anti-oxidant activity (generating H 2O 2) than did gallic acid and gallic acid methyl esters. However, gallic acid inhibited the formation of H 2O 2, due to the peroxidation reaction with its carboxylic group, which generated O 2.
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