Polyphenoloxidase from Riesling and Dornfelder wine grapes (Vitis vinifera) is a tyrosinase

Fronk, Petra; Hartmann, Hermann; Bauer, Margarita; Solem, Even; Jaenicke, Elmar; Decker, Heinz

doi:10.1016/j.foodchem.2015.03.016

Cited by 45 publications

(36 citation statements)

References 48 publications

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“…Catechol oxidases, also known as o -diphenol oxidases, catalyse the oxidation of o -diphenols to o -quinones. Finally, laccases are capable to oxidize a wide spectrum of aromatic compounds by a radical catalysed reaction mechanism [12]. …”

Section: Polyphenol Oxidases (Ppo) and Browningmentioning

confidence: 99%

“…PPOs have been extensively studied with respect to physico-chemical properties [10,11,12,13] and PPO isoenzymes can be distinguished based on electrophoretic mobility, optimal temperature and pH and substrate specificity [14,15,16,17]. PPO activity depends on the pH, which affects the binding of substrates and the catalysis [18,19,20].…”

Section: Polyphenol Oxidases (Ppo) and Browningmentioning

confidence: 99%

“…JrPPO1 encodes a functional enzyme expressed primarily in the leaves, hulls, and flowers, whereas JrPPO 2 is more expressed in callus tissues and in roots [8,9,10,11,12,13,14,15,16,17,18,19,20,21,22,23,24,25,26,27,28,29,30,31,32,33,34,35,36,37,38,39,40,41,42,43,44,45,46,47,48,49,50,51,52,53,54,55,56,57,58,59,60,61,62,63,64,65,66,67,68,69,70,71,72,73,74,75,76,77,78,79,80…”

Section: Genomic and Genetic Aspectsmentioning

confidence: 99%

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Polyphenol Oxidases in Crops: Biochemical, Physiological and Genetic Aspects

Taranto

Pasqualone

Mangini

et al. 2017

IJMS

325

187

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Enzymatic browning is a colour reaction occurring in plants, including cereals, fruit and horticultural crops, due to oxidation during postharvest processing and storage. This has a negative impact on the colour, flavour, nutritional properties and shelf life of food products. Browning is usually caused by polyphenol oxidases (PPOs), following cell damage caused by senescence, wounding and the attack of pests and pathogens. Several studies indicated that PPOs play a role in plant immunity, and emerging evidence suggested that PPOs might also be involved in other physiological processes. Genomic investigations ultimately led to the isolation of PPO homologs in several crops, which will be possibly characterized at the functional level in the near future. Here, focusing on the botanic families of Poaceae and Solanaceae, we provide an overview on available scientific literature on PPOs, resulting in useful information on biochemical, physiological and genetic aspects.

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Section: Polyphenol Oxidases (Ppo) and Browningmentioning

confidence: 99%

Section: Polyphenol Oxidases (Ppo) and Browningmentioning

confidence: 99%

Section: Genomic and Genetic Aspectsmentioning

confidence: 99%

See 1 more Smart Citation

Polyphenol Oxidases in Crops: Biochemical, Physiological and Genetic Aspects

Taranto

Pasqualone

Mangini

et al. 2017

IJMS

325

187

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“…1.10.3.2) has no monohydroxylase activity, and oxidizes a broad spectrum of different phenols and other compounds by a radical mechanism. Tyrosinase originates from grape berries [84], whereas laccases in must and wine are derived from epiphytic fungi, particularly Botrytis cinerea [82]. Phenolic compounds as caffeic acid, gallic acid, vanillic acid, ferulic acid, or especially resveratrol are known for their beneficial effects on human health.…”

Section: Phenoloxidasesmentioning

confidence: 99%

Enzymes for Wine Fermentation: Current and Perspective Applications

Claus

Mojsov

2018

Fermentation

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Enzymes are used in modern wine technology for various biotransformation reactions from prefermentation through fermentation, post-fermentation and wine aging. Industrial enzymes offer quantitative benefits (increased juice yields), qualitative benefits (improved color extraction and flavor enhancement) and processing advantages (shorter maceration, settling and filtration time). This study gives an overview about key enzymes used in winemaking and the effects of commercial enzyme preparations on process engineering and the quality of the final product. In addition, we highlight on the presence and perspectives of beneficial enzymes in wine-related yeasts and lactic acid bacteria.

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“…However, during MD simulations the classical tyrosinase substrate tyramine is destabilized in the active center of plant PPOs by an arginine in this position (AUS1, L244R mutant of jrTYR), whereas it is stabilized by a leucine in this position (jrTYR). It has been reported recently that vvCO, possessing a lysine in this position, showed weak activity toward tyrosine and tyramine, and vvCO was therefore classified as a tyrosinase (46). However, a comparison of the kinetic data of vvCO and jrTYR indicates that tyramine will presumably not be the natural substrate of vvCO [K m (vvCO) = 7.7 mM (46); K m (jrTYR) = 0.274 mM (23)].…”

Section: Reactivity Of Aus1 and Insights Into The Reaction Mechanism mentioning

confidence: 99%

Aurone synthase is a catechol oxidase with hydroxylase activity and provides insights into the mechanism of plant polyphenol oxidases

Molitor

Mauracher

Rompel

2016

Proc. Natl. Acad. Sci. U.S.A.

121

109

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Tyrosinases and catechol oxidases belong to the family of polyphenol oxidases (PPOs). Tyrosinases catalyze the o-hydroxylation and oxidation of phenolic compounds, whereas catechol oxidases were so far defined to lack the hydroxylation activity and catalyze solely the oxidation of o-diphenolic compounds. Aurone synthase from Coreopsis grandiflora (AUS1) is a specialized plant PPO involved in the anabolic pathway of aurones. We present, to our knowledge, the first crystal structures of a latent plant PPO, its mature active and inactive form, caused by a sulfation of a copper binding histidine. Analysis of the latent proenzyme's interface between the shielding C-terminal domain and the main core provides insights into its activation mechanisms. As AUS1 did not accept common tyrosinase substrates (tyrosine and tyramine), the enzyme is classified as a catechol oxidase. However, AUS1 showed hydroxylase activity toward its natural substrate (isoliquiritigenin), revealing that the hydroxylase activity is not correlated with the acceptance of common tyrosinase substrates. Therefore, we propose that the hydroxylase reaction is a general functionality of PPOs. Molecular dynamics simulations of docked substrate-enzyme complexes were performed, and a key residue was identified that influences the plant PPO's acceptance or rejection of tyramine. Based on the evidenced hydroxylase activity and the interactions of specific residues with the substrates during the molecular dynamics simulations, a novel catalytic reaction mechanism for plant PPOs is proposed. The presented results strongly suggest that the physiological role of plant catechol oxidases were previously underestimated, as they might hydroxylate their-so far unknown-natural substrates in vivo.crystal structure | tyrosinase | catechol oxidase | type III copper protein | mechanism

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Polyphenoloxidase from Riesling and Dornfelder wine grapes (Vitis vinifera) is a tyrosinase

Cited by 45 publications

References 48 publications

Polyphenol Oxidases in Crops: Biochemical, Physiological and Genetic Aspects

Polyphenol Oxidases in Crops: Biochemical, Physiological and Genetic Aspects

Enzymes for Wine Fermentation: Current and Perspective Applications

Aurone synthase is a catechol oxidase with hydroxylase activity and provides insights into the mechanism of plant polyphenol oxidases

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