Inhibition of polyphenol oxidase obtained from various sources by 2,3‐diaminopropionic acid

Abstract

Abstract This paper reports for the first time the inhibition of the catecholase activities of mushroom, artichoke ( Cynara scolymus L) and Ocimum basilicum L polyphenol oxidase by 2,3‐diaminopropionic acid. Polyphenol oxidases from artichoke and O basilicum L were purified by ammonium sulfate precipitation, dialysis and a Sepharose 4B‐ L ‐tyrosine‐ p ‐aminobenzoic acid‐affinity column. In inhibition studies, 2,3‐diaminopropionic acid showed uncompetitive inhibition for mushroom PPO using catechol and pyrogallol as substrates, competitive inhibition for O basilicum L PPO using catechol as a substrate, and uncompetitive inhibition for artichoke PPO using catechol as a substrate. Furthermore, sodium azide, which is an inhibitor of PPO, was used as an inhibitor for comparison with the inhibition potency of 2,3‐diaminopropionic acid. The highest 2,3‐diaminopropionic acid inhibition observed with O basilicum L ( K i = 0.89 m M ), followed by artichoke ( K i = 1.42 m M ) and mushroom ( K i = 2.47 m M ), respectively. Copyright © 2005 Society of Chemical Industry