Inhibitory effect of coumarin derivatives on apple (cv. Idared) polyphenol oxidase

Abstract

Inhibitory effect of 32 coumarin derivatives (20 Schiff bases, 5 thiosemicarbazides, 5 thiazolidinones, and their precursors, 7-hydroxy-4-methylcoumarin and 4-methylcoumarin-7-yl hydrazine carboxylate) on partially purified apple polyphenol oxidase was investigated. Thirteen coumarin derivatives inhibited polyphenol oxidase (5 Schiff bases, 5 thiosemicarbazides, 1 thiazolidinone, 4-methyl-7-hydroxycoumarin and 4-methylcoumarin-7-yl hydrazine carboxylate), while 19 derivatives showed no effect on enzyme activity. The most effective inhibitors were thiosemicarbazides, with 4-methyl-1-(2-(4-methyl-2-oxo-2H-chromen-7-yloxy)acetyl) thiosemicarbazide (compound C23) being the most prominent inhibitor (IC50 = 10.45 µM). The importance of thiosemicarbazide moiety as crucial structure element for strong apple PPO inhibition was confirmed by its cyclisation to thiazolidinone bearing the same substituents as corresponding thiosemicarbazide. Capture of the sulphur atom of thiosemicarbazide group within tiazolidinone ring caused significant loss of inhibitory effect against apple PPO.