There has been considerable interest in controlling polyphenol oxidase (PPO) activity to prevent enzymatic browning in foods. However, studies on inhibitions of different forms of PPO are very limited. Thus, this study focuses on the effects of cinnamic acid, β-cyclodextrin, L-cysteine, and ascorbic acid on soluble PPO (sPPO) and membrane-bound PPO (mPPO) in peach fruit. The activity of partially purified sPPO was 3.17 times higher than that of mPPO. However, mPPO was shown to be more stable than sPPO in the presence of inhibitors with different concentrations (i.e., 1, 3, 5 mM); activation of mPPO was found by 5 mM L-cysteine. Both sPPO and mPPO inhibitions were PPO substrate-dependent. Ascorbic acid showed the highest inhibitory effect on both sPPO and mPPO with all studied inhibitors and substrates. The inhibition of 1 mM ascorbic acid on sPPO and mPPO reached 95.42 ± 0.07% and 65.60 ± 1.16%, respectively. β-Cyclodextrin had a direct inhibitory effect only on sPPO, while the other three inhibitors had direct effects on both sPPO and mPPO. Cinnamic acid exhibited a non-competitive inhibition on sPPO and mPPO, with L-cysteine showing the same, though on sPPO. The inhibition of studied inhibitors on sPPO and mPPO is highly related to the substrate environment, type, and concentration of inhibitors. This study provides a basis for the further prevention of peach fruit browning from the perspective of different enzyme forms.

Thinned peach polyphenols (TPPs) were extracted by ultrasonic disruption and purified using macroporous resin. Optimized extraction conditions resulted in a TPPs yield of 1.59 ± 0.02 mg GAE/g FW, and optimized purification conditions resulted in a purity of 43.86% with NKA-9 resin. TPPs composition was analyzed by UPLC-ESI-QTOF-MS/MS; chlorogenic acid, catechin, and neochlorogenic acid were the most abundant compounds in thinned peaches. Purified TPPs exhibited scavenging activity on DPPH, ABTS, hydroxyl radical, and FRAP. TPPs inhibited α-amylase and α-glucosidase by competitive and noncompetitive reversible inhibition, respectively. TPPs also exhibited a higher binding capacity for bile acids than cholestyramine. In summary, TPPs from thinned peaches are potentially valuable because of their high antioxidant, hypoglycemic, and hypolipidemic capacities, and present a new incentive for the comprehensive utilization of thinned peach fruit.

There has been considerable interest in using natural polyphenol oxidase (PPO) inhibitors to control browning in fruit and vegetable products. p-Coumaric acid (pCA), a common secondary metabolite of plants, has been studied as an inhibitor of PPOs/tyrosinases from several foods (e.g., mushroom, apple, and potato). However, studies on the use of pCA for the inhibition of PPO-initiated browning in actual food systems are limited. Therefore, a study was carried out to ascertain the efficacy of using pCA to limit PPO-initiated browning in fresh potato juice. The extent of browning inhibition by pCA was shown to be reaction system-dependent. Browning in potato juice was unexpectedly enhanced by the addition of pCA. This was interpreted as pCA acting as an alternative substrate with significantly higher browning efficiency; extent of browning under this condition was higher than that observed in the native potato juice. The addition of pCA to any of the model reaction mixtures (i.e., those containing semi-purified enzymes and substrates) significantly inhibited browning. The discrepancy in pCA effects on browning inhibition in different reaction systems is postulated to be mainly due to non-enzyme and non-substrate components in potato juice that participate in the post-PPO reaction sequences, which ultimately lead to brown color formation.