Differential in vitro inhibition of polyphenoloxidase from a wild edible mushroom Lactarius salmonicolor

Abstract

The polyphenol oxidase (LsPPO) from a wild edible mushroom Lactarius salmonicolor was purified using a Sepharose 4B-Ltyrosine-p-amino benzoic acid affinity column. At the optimum pH and temperature, the K M and V Max values of LsPPO towards catechol, 4-methylcatechol and pyrogallol were determined as 0.025 M & 0.748 EU/mL, 1.809 £ 10 23 M & 0.723 EU/mL and 9.465 £ 10 23 M & 0.722 EU/mL, respectively. Optimum pH and temperature values of LsPPO for the three substrates above ranged between the pH 4.5-11.0 and 5-508C. Enzyme activity decreased due to heat denaturation with increasing temperature. Effects of a variety of classical PPO inhibitors were investigated opon the activity of LsPPO using catechol as the substrate. IC 50 values for glutathione, p-aminobenzenesulfonamide, L-cysteine, L-tyrosine, oxalic acid, b-mercaptoethanol and syringic acid were determined as 9.1 £ 10 24 , 2.3 £ 10 24 M, 1.5 £ 10 24 M, 3.8 £ 10 27 M, 1.2 £ 10 24 M, 4.9 £ 10 24 M, and 4 £ 10 24 M respectively. Thus L-tyrosine was by far the most effective inhibitor. Interestingly, sulfosalicylic acid behaved as an activator of LsPPO in this study.

Inhibitory effect of chemical and natural anti-browning agents on polyphenol oxidase from ginger (Zingiber officinale Roscoe)

“…In this study, mixed-type inhibition and un-competitive-type inhibition of L-cysteine on ginger PPO using 4-methylcatechol and pyrocatechol, respectively were observed (Table 1). Inhibition of polyphenol oxidase activity by Lcysteine has been reported in browning control of acanthus PPO (Saeidian 2016) and wild mushroom PPO (Dedeoglu and Guler 2009).…”

Using of group‐based selected flavonoids as alternative inhibitors for potato polyphenol oxidase

“…for pPPO enzyme and a noncompetitive inhibition was observed using chlorogenic acid (o-diphenol) as a substrate (Macrae & Dugglegy, 1968). Authors also reported that syringic acid exhibited uncompetitive inhibition with the K i value of 21 µM for PPO obtained from Lactarius salmonicolor (Dedeoglu & Guler, 2009). In another study, authors observed K i value at 64.1 µM with quercetin for mushroom tyrosinase (Fan et al, 2017) and K i value at 88 µM with quercetin for Sarcophaga bullata PPO (Wang et al, 2004).…”

“…The detailed purification profile was given in Table 1. In the literature, PPO was purified 26.6-fold from a wild edible mushroom (Dedeoglu & Guler, 2009) and 19.77-fold from tea leaves (Öztürk et al, 2020) using this method allowing efficient purification.…”

The Effect of Dielectric Barrier Discharge Plasma Gas and Plasma-Activated Water on the Physicochemical Changes in Button Mushrooms (Agaricus bisporus)

“…The PPO activity of the untreated mushrooms and those exposed to ACP for 20 min were measured according to a procedure described by Dedeoglu et al [ 20 ] with minor modifications, using catechol as the substrate. After cold plasma treatment, 5 mg of button mushroom frozen powder was homogenized in 100 mL of sodium phosphate buffer (0.05 M, pH7.4).…”