Biochemical and Immunochemical Characteristics of Polyphenol Oxidases from Different Fruits of Prunus

Fraignier, Marie-Pierre; Marqués, L. Pons; Fleuriet, Annie; Macheix, Jean‐Jacques

doi:10.1021/jf00057a011

Cited by 69 publications

(61 citation statements)

References 27 publications

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“…In the literature there are different reports about the number of PPO isoforms in apricots. For example, Vamos-Vigyazo (18) reported the existence of two main enzyme fractions in these fruits, whereas Chavalier et al (30) and Fraignier et al (31) reported the presence of a single main and several minor forms. Thus, it appears that the apricots may contain different numbers of PPO molecular forms.…”

Section: Characterization Of Ts-ppomentioning

confidence: 99%

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Consistency of Polyphenol Oxidase (PPO) Thermostability in Ripening Apricots (Prunus armeniaca L.): Evidence for the Presence of Thermostable PPO Forming and Destabilizing Mechanisms in Apricots

Yemenicioğlu

Cemeroğlu

2003

J. Agric. Food Chem.

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Destabilization of thermostable polyphenol oxidase (TS-PPO) during the ripening of peaches has been previously shown (Yemenicioǧ lu, A.; Cemeroǧ lu, B. Tr. J. Agric. For. 1998, 22, 261-265). This work studied the effect of ripening on thermal stability of apricot PPO for three different cultivars. Kabaaş ı cultivar contained thermolabile PPO, whereas TS-PPO appeared in Hacıhaliloǧ lu and Ç ataloǧ lu cultivars. The TS-PPO showed biphasic inactivation curves, and its D and z values between 60 and 90°C varied in the ranges of 357-1.12 min and 11.9-12.7°C, respectively. In Hacıhaliloǧ lu cultivar the TS-PPO was very consistent and existed at all stages of ripening, whereas in Ç ataloǧ lu cultivar it appeared only at the half-ripe stage. The loss of consistent TS-PPO in Hacıhaliloǧ lu apricots after partial purification by acetone precipitation and DEAE-cellulose chromatography suggested the non-covalent nature of its stabilization. The main purified fractions (F1 and F2) showed monophasic inactivation curves with similar thermal inactivation parameters (z F1 ) 10.4°C, z F2 ) 10.1°C). However, their kinetic properties against catechol (K mF1 ) 61 mM, K mF2 ) 122.7 mM) and substrate specificities were considerably different. The results of this study showed the presence of TS-PPO forming and destabilizing mechanisms in apricots. Further studies are needed for the solution of these mechanisms and to develop some new strategies that may be utilized by molecular techniques for a planned production of apricot cultivars provided with heat labile but normal PPO activity.

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Section: Characterization Of Ts-ppomentioning

confidence: 99%

“…Fraignier et al (31) reported that in apricots and in other Prunus fruits the main active PPO form is a 43 kDa enzyme. The possible high molecular weight precursor of this enzyme form detected with apple anti-PPO antibodies was an inactive protein of 63 kDa molecular weight.…”

Section: Characterization Of Ts-ppomentioning

confidence: 99%

Consistency of Polyphenol Oxidase (PPO) Thermostability in Ripening Apricots (Prunus armeniaca L.): Evidence for the Presence of Thermostable PPO Forming and Destabilizing Mechanisms in Apricots

Yemenicioğlu

Cemeroğlu

2003

J. Agric. Food Chem.

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“…Fenoles, actividad fenolasa y disponibilidad de sustrato el oscurecimiento enzimático de los tejidos, causado por la oxidación de compuestos fenólicos para formar quinonas, está principalmente catalizado por las PPos (Fraignier et al 1995), y la tasa de oxidación fenólica puede ser disminuida mediante una reducción en la actividad de las enzimas oxidativas o mediante la disminución del sustrato disponible para su oxidación (george 1996). como la actividad de las enzimas relacionadas con la biosíntesis y la oxidación de los fenoles puede ser manipulada, y disminuye en ausencia de luz, en diversos estudios (Villalobos y arias 1987, marks y simpson 1990, Pirela 1996, sudripta et al 1996, seneviratne y Wijesekara 1996, León et al 1997, se incluyó el acondicionamiento del material donante o de los explantes establecidos in vitro a crecimiento en oscuridad durante cierto tiempo a fin de lograrlo.…”

Section: +unclassified

Problemas de oxidación y oscurecimiento de explantes cultivados in vitro

Azofeifa

2008

Agron. Mesoam.

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“…In addition, quinones can be obtained by autoxidation or chemical oxidation (Guyot et al, 1996). Although valued in tea and wine processing, browning reactions are particularly detrimental for fresh fruits and vegetables (Fraignier et al, 1995). Moreover, the coupling of phenols in the presence of catechol oxidase is responsible for browning and cloudiness in beverages (Guyot et al, 1996).…”

Section: Introductionmentioning

confidence: 99%

TRANSPARENT TESTA10 Encodes a Laccase-Like Enzyme Involved in Oxidative Polymerization of Flavonoids in Arabidopsis Seed Coat

Pourcel

Routaboul

Kerhoas³

et al. 2005

The Plant Cell

416

424

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The Arabidopsis thaliana transparent testa10 (tt10) mutant exhibits a delay in developmentally determined browning of the seed coat, also called the testa. Seed coat browning is caused by the oxidation of flavonoids, particularly proanthocyanidins, which are polymers of flavan-3-ol subunits such as epicatechin and catechin. The tt10 mutant seeds accumulate more epicatechin monomers and more soluble proanthocyanidins than wild-type seeds. Moreover, intact testa cells of tt10 cannot trigger H 2 O 2 -independent browning in the presence of epicatechin and catechin, in contrast with wild-type cells. UVvisible light detection and mass spectrometry revealed that the major oxidation products obtained with epicatechin alone are yellow dimers called dehydrodiepicatechin A. These products differ from proanthocyanidins in the nature and position of their interflavan linkages. Flavonol composition was also affected in tt10 seeds, which exhibited a higher ratio of quercetin rhamnoside monomers versus dimers than wild-type seeds. We identified the TT10 gene by a candidate gene approach. TT10 encodes a protein with strong similarity to laccase-like polyphenol oxidases. It is expressed essentially in developing testa, where it colocalizes with the flavonoid end products proanthocyanidins and flavonols. Together, these data establish that TT10 is involved in the oxidative polymerization of flavonoids and functions as a laccase-type flavonoid oxidase.

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Biochemical and Immunochemical Characteristics of Polyphenol Oxidases from Different Fruits of Prunus

Cited by 69 publications

References 27 publications

Consistency of Polyphenol Oxidase (PPO) Thermostability in Ripening Apricots (Prunus armeniaca L.): Evidence for the Presence of Thermostable PPO Forming and Destabilizing Mechanisms in Apricots

Consistency of Polyphenol Oxidase (PPO) Thermostability in Ripening Apricots (Prunus armeniaca L.): Evidence for the Presence of Thermostable PPO Forming and Destabilizing Mechanisms in Apricots

Problemas de oxidación y oscurecimiento de explantes cultivados in vitro

TRANSPARENT TESTA10 Encodes a Laccase-Like Enzyme Involved in Oxidative Polymerization of Flavonoids in Arabidopsis Seed Coat

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