Novel Procedure for Extraction of a Latent Grape Polyphenoloxidase Using Temperature-Induced Phase Separation in Triton X-114

Sánchez‐Ferrer, Álvaro; Bru, Roque; García‐Carmona, Francisco

doi:10.1104/pp.91.4.1481

Cited by 110 publications

(72 citation statements)

References 34 publications

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“…This agrees with the report of others (2,18) The presence of peroxidase and PPO in peach has been described earlier (13). PPO is a membrane protein which is activated by disruption and attack by proteolytic enzymes (16). As shown in Figure 1C, PPO Peroxidases are involved in the last step in lignin formation.…”

Section: Discussionmentioning

confidence: 99%

Characterization of Peroxidases in Lignifying Peach Fruit Endocarp

Abeles¹,

Biles²

1991

Plant Physiol.

203

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Developing peach (Prunus persica L. Batsch 'Redskin') fruit were used to characterize the role of peroxidases in lignification. During development, the endocarp of these drupes becomes lignified while the mesocarp remains parenchymatous. Acidic peroxidase from lignifying endocarp were similar to those of the fleshy mesocarp. The endocarp had a larger amount and number of basic peroxidases than the mesocarp. Cultured peach leaf cells are thought to be lignified because their walls give a positive reaction with phloroglucinol-HCI. These cells also secreted a basic peroxidase. Peroxidases were difficult to extract from en-

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Section: Discussionmentioning

confidence: 99%

Characterization of Peroxidases in Lignifying Peach Fruit Endocarp

Abeles¹,

Biles²

1991

Plant Physiol.

203

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“…PPO was extracted from grape berries in a latent form by using temperature-induced phase separation in Triton X-1 14 at pH 7.3 (14). The solution thus obtained, after dialysis against 1 mm sodium phosphate buffer (pH 7.3), was used as enzyme source.…”

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

“…A new method has been developed that permits the extraction ofPPO in this latent state by using temperatureinduced phase separation in Triton X-1 14 (14). The latent enzyme can be activated by different treatments such as trypsin (14,17), fatty acids (4), aging (8), acid and base shock (5,6), detergents (1 1, 15), and cations (16). As regards activation of the enzyme by pH changes in the medium, this phenomenon was first studied by Kenten (5) It has been shown that some enzymes located in cell envelopes display different kinetic behavior depending on the pH of the medium, which may represent a regulatory device operative in vivo (3).…”

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confidence: 99%

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Hysteresis and Cooperative Behavior of a Latent Plant Polyphenoloxidase

Valero¹,

García-Carmona²

1992

Plant Physiol.

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Appearance of a lag period dependent on pH in the expression of the catecholase activity of a polyphenoloxidase extracted in a latent state from Airen grape (Vitis vinifera L.) berries, is revealed, suggesting the hysteretic nature of the enzyme. The lag time was independent of enzyme concentration, indicating that slow pHinduced conformational changes in the protein must occur during assay. Results obtained by varying substrate concentration show that the system presents hyperbolic or cooperative kinetics depending on the pH of the assay.PPo2 (EC 1.14.18.1.) is a copper-containing monooxygenase widely distributed in nature that is responsible for melanization in animals and browning in plants. The enzyme catalyzes two distinct reactions involving molecular oxygen, namely (a) the o-hydroxylation of monophenols to o-diphenols, or cresolase activity, and (b) the subsequent oxidation of o-diphenols to o-quinones, or catecholase activity.

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“…para su solubilización: detergentes como Tritón X-100, (Harel y Mayer, 1971), Tritón X-114 (Sánchez-Ferrer et al, 1989), enzimas proteolíticas (Mayer, 1966), etc. Algunos tratamientos pueden alterar la estructura y la conformación de la enzima provocando el paso de su forma inactiva o latente a su forma activa (Kenten, 1958), si bien la recuperación de la enzima nativa latente es posible mediante el uso de detergentes no iónicos suaves (Sánchez-Ferrer et al,, 1994).…”

Section: Ciencia Y Tecnología 2014 7(1):23-31unclassified

Distribución, Localización E Inhibidores De Las Polifenol Oxidasas en Frutos Y Vegetales Usados Como Alimento

Carriel

Agnieszka-Obrebska

Bru-Martínez

et al. 2014

CyT

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. Quito km, 1.5 vía a Santo Domingo de los Tsáchilas. EC-120501. Quevedo, Ecuador. rpico@uteq.edu.ec resumen L as polifenol oxidasas (PPOs) son enzimas ubicuas que catalizan la reacción dependiente de oxígeno que transforma o-difenoles en o-quinonas. Estas quinonas son reactivas y capaces de modificar covalentemente un amplio abanico de especies nucleófilas, del interior de las células, que conduce a la formación de polímeros marrones, conocido como pardeamiento enzimático. El fenómeno de pardeamiento durante el crecimiento, recogida, almacenamiento y procesado de frutos y vegetales, es un problema de primera magnitud en la industria agroalimentaria y se reconoce como una de las principales causas de pérdidas de calidad y valor comercial. Produce cambios importantes tanto en la apariencia como en las propiedades organolépticas de frutos y vegetales comestibles, además suele ir asociado al desprendimiento de olores y efectos negativos sobre el valor nutricional. Aunque las PPOs se han descrito en diversos tejidos de plantas como raíces, semillas, hojas y frutos, el control de este fenómeno requiere un conocimiento bioquímico del tipo de sustratos fenólicos presentes en cada planta, el nivel de compuestos reductores, el nivel de accesibilidad del O 2 , de la naturaleza de los diferentes compuestos oxidables y de la polimerización y degradación de las o-quinonas. En este trabajo se presenta una revisión del efecto bioquímico, distribución, localización y posibles inhibidores de las PPOs en frutos y vegetales usados como alimento.Palabras clave: Polifenol oxidasas, pardeamiento enzimático, frutos y vegetales. abstract P olyphenol oxidases (PPOs) are ubiquitous enzymes that catalyze the oxygen-dependent reaction that transforms o-diphenols to o-quinones. These quinones are reactive and capable of covalently modifying a wide variety of nucleophilic species into cells leading to the formation of brown polymers, known as enzymatic browning. The phenomenon of browning during growth, collection, storage and processing of fruits and vegetables, is a major problem in the food industry and is recognized as one of the leading causes of commercial value and quality loss, since it produces important changes in the appearance and organoleptic properties of edible fruits and vegetables, and it is often associated to the release of odors and negative effects on nutritional value. Although PPOs have been described in various plant tissues such as roots, sedes, leaves and fruits, the control of this phenomenon requires biochemical knowledge of the type of phenolic substrates present in each plant, the level of reducing compounds, the level of O 2 accessibility, of the nature of the various oxidizable compounds and, finally, o-quinones polymerization and degradation. This paper present a review of the biochemical effect, distribution, location and potential inhitors of PPOs in fruits used for food.

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Novel Procedure for Extraction of a Latent Grape Polyphenoloxidase Using Temperature-Induced Phase Separation in Triton X-114

Cited by 110 publications

References 34 publications

Characterization of Peroxidases in Lignifying Peach Fruit Endocarp

Characterization of Peroxidases in Lignifying Peach Fruit Endocarp

Hysteresis and Cooperative Behavior of a Latent Plant Polyphenoloxidase

Distribución, Localización E Inhibidores De Las Polifenol Oxidasas en Frutos Y Vegetales Usados Como Alimento

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