Chlorogenic acid is the ma
jor diphenol of many fruits, where it is oxidized enzymatically by polyphenoloxidase (PPO) or peroxidase (POD) to its
o-quinone. In spectrophotometric studies of chlorogenicacid oxidation with a periodate ratio of [CGA]
0/[IO
4-]
0 < 1 and [CGA]
0/[IO
4-]
0 > 1, the
o-quinone wascharacterized as follows:
max at 400 nm and
= 2000 and 2200 M
-1 cm
-1 at pH 4.5 and 7.0,respectively. In studies of
o-quinone generated by the oxidation of chlorogenic acid using a periodateat ratio of [CGA]
0/[IO
4-]
0 > 1, a reaction with the remaining substrate was detected, showing rateconstants of
k = 2.73 ± 0.17 M
-1 s
-1 and
k' = 0.05 ± 0.01 M
-1 s
-1 at the above pH values. Achronometric spectrophotometric method is proposed to kinetically characterize the action of the PPOor POD on the basis of measuring the time it takes for a given amount of ascorbic acid to be consumedin the reaction with the
o-quinone. The kinetic constants of mushroom PPO and horseradish PODare determined.