Purification and Characterization of Dog-rose (<i>Rosa </i><i>dumalis</i> Rechst.) Polyphenol Oxidase

Şakiroğlu, Halis; Küfrevioğlu, Ömer İrfan; Kocaçalışkan, İsmail; Oktay, and Münir; Onganer, Yavuz

doi:10.1021/jf950808g

Cited by 46 publications

(26 citation statements)

References 26 publications

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“…This observation was similar to that of the work on PPO from dog-rose [21], ferula sp. [22], and Amasya apple [28].…”

Section: Enzyme Kinetics and Substrate Specificitysupporting

confidence: 90%

“…It is found that the optimum temperature is 108C for catechol and chlorogenic acid, and 558C for dopamine. It is reported that optimum temperature for PPO is 158C for Amasya apple [28], 208C for DeChaunac grape [53], 258C for dog-rose [21], 308C for aubergine [45], 128C for Ferula sp. [22], and 408C for Chinese cabbage [55], using catechol as a substrate, 208C for dog-rose [21], 308C for aubergine [45], 258C for Ferula sp.…”

Section: Effect Of Temperature On Activitymentioning

confidence: 99%

“…It is reported that optimum temperature for PPO is 158C for Amasya apple [28], 208C for DeChaunac grape [53], 258C for dog-rose [21], 308C for aubergine [45], 128C for Ferula sp. [22], and 408C for Chinese cabbage [55], using catechol as a substrate, 208C for dog-rose [21], 308C for aubergine [45], 258C for Ferula sp. [22], and 568C for Amasya apple [29], using 4-methylcatechol as a substrate, and 158C for dog-rose [21] and 708C for Amasya apple [28] using pyrogallol as a substrate.…”

Section: Effect Of Temperature On Activitymentioning

confidence: 99%

“…[22], and 408C for Chinese cabbage [55], using catechol as a substrate, 208C for dog-rose [21], 308C for aubergine [45], 258C for Ferula sp. [22], and 568C for Amasya apple [29], using 4-methylcatechol as a substrate, and 158C for dog-rose [21] and 708C for Amasya apple [28] using pyrogallol as a substrate.…”

Section: Effect Of Temperature On Activitymentioning

confidence: 99%

“…There are many works related to PPO from different plants such as wheat [15], Allium sp. [19], sorghum [17], Beta vulgaris L. [18], tea leaf [19], lettuce [20], dog-rose [21], Ferula sp. [22], Anethum graveolens L. [23], peaches [24], apples [25,26,27,28], grapes [29,30,31], kiwis [32], Salvia species [33] and Thymus [34].…”

Section: Introductionmentioning

confidence: 99%

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Some kinetic properties of polyphenol oxidase obtained from dill (Anethum graveolens)

Şakiroğlu

Öztürk

Pepe

et al. 2008

Journal of Enzyme Inhibition and Medicinal Chemistry

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Polyphenol oxidase (PPO) was partially purified from dill by (NH 4 ) 2 SO 4 precipitation followed by dialysis and gel filtration chromatography. Polyphenol oxidase activity was measured spectrophotometrically at 420 nm using catechol, dopamine and chlorogenic acid as substrates. Optimum pH, temperature, and ionic strength were determined with three substrates. The best substrate of dill PPO was found to be chlorogenic acid. Some kinetic properties of the enzyme such as V max, K M and V max /K M were determined for all three substrates. The effects of various inhibitors on the reaction catalysed by the enzyme were tested and I 50 values calculated. The most effective inhibitor was L-cysteine. Activation energies, E a , were determined from the Arrhenius equation. In addition, activation enthalpy, DH a , and Q 10 values of the enzyme were also calculated.

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“…This observation was similar to that of the work on PPO from dog-rose [21], ferula sp. [22], and Amasya apple [28].…”

Section: Enzyme Kinetics and Substrate Specificitysupporting

confidence: 90%

Section: Effect Of Temperature On Activitymentioning

confidence: 99%

Section: Effect Of Temperature On Activitymentioning

confidence: 99%

Section: Effect Of Temperature On Activitymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Some kinetic properties of polyphenol oxidase obtained from dill (Anethum graveolens)

Şakiroğlu

Öztürk

Pepe

et al. 2008

Journal of Enzyme Inhibition and Medicinal Chemistry

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Browning in processed yams: peroxidase or polyphenol oxidase?

et al. 2002

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Polyphenol oxidase and peroxidase were puri®ed from white yam (Dioscorea rotundata) using DEAE-cellulose ionexchange chromatography. Thermoinactivation curves for polyphenol oxidase showed monophasic kinetics, while those for peroxidase were biphasic. Urea partially stabilised peroxidase against irreversible thermoinactivation, but did not do so in the case of polyphenol oxidase. Only peroxidase was capable of regenerating activity after thermoinactivation. The results showed that thermoinactivation of peroxidase was mainly due to conformational changes, while that of polyphenol oxidase was probably due to covalent damage. Peroxidase reactivation might play an important role in the browning of processed yam. INTRODUCTIONDespite the importance of yam as a major food crop in West Africa, its postharvest biochemistry has been poorly studied. 1 As a consequence, postharvest losses due to sprouting, physical damage, pests and pathogens have remained relatively high. 2 One relatively successful procedure for improving the postharvest storage of white yam (Dioscorea rotundata) tubers involves processing into¯our. This consists of (1) peeling off the outer covering, (2) cubing, (3) boiling in distilled water for 10±15 min, (4) drying and (5) milling into¯our. Unfortunately, consumer acceptability and the shelf-life of the¯our are adversely affected by the inability of the¯our to retain the typical white colour of yam which is highly desired by consumers. 3,4 Colour changes in freshly damaged plant materials have been attributed to the activity of polyphenol oxidase (PPO; o-diphenol:O 2 oxidoreductase, EC 1.10.3.2), which catalyses the oxidation of polyphenols to o-quinones. 5,6 Peroxidase (Px; donor: hydrogen peroxide oxidoreductase, EC 1.11.1.7) catalyses the oxidation of a number of aromatic compounds and has been associated with darkening in fresh and processed vegetables and fruits. 7 Both PPO and Px are known to be highly heat-resistant but each displays a different capability for reactivation after thermoinactivation. 5,8±11In D rotundata, which contains PPO, 3,4,12 correlating PPO activity with tissue browning was shown to be contraindicative. 13 The purpose of the present study was to relate the thermoinactivation processes of PPO and Px to the discolouration of processed yam.

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Characterization of polyphenol oxidase from Uapaca kirkiana fruit

et al. 2005

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Polyphenol oxidase (PPO), the enzyme responsible for the postharvest spoilage of fruits, was extracted and purified from Uapaca kirkiana peel and pulp by ammonium sulfate precipitation and dialysis. Further purification of peel PPO was carried out by gel filtration chromatography. Optimum pH values were 7 and 8 for peel and pulp PPO, respectively. The optimum temperatures for peel and pulp PPO were 45 and 35 • C, respectively. Inhibition studies of the PPO enzyme were performed using citric acid, sodium azide, sodium metabisulfite and thiourea. The most effective inhibitors were sodium azide and citric acid for both peel and pulp PPO. V max and K m values were 13.63 units min −1 and 4.923 mmol L −1 , respectively, for peel PPO and 14.03 units min −1 and 5.43 mmol L −1 , respectively, for pulp PPO. Three isoenzymes of Uapaca kirkiana PPO were detected by polyacrylamide gel electrophoresis. One of the isoenzymes could be identified as having a molecular weight of 26 625 Da.

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Purification and Characterization of Dog-rose (Rosa dumalis Rechst.) Polyphenol Oxidase

Cited by 46 publications

References 26 publications

Some kinetic properties of polyphenol oxidase obtained from dill (Anethum graveolens)

Some kinetic properties of polyphenol oxidase obtained from dill (Anethum graveolens)

Browning in processed yams: peroxidase or polyphenol oxidase?

Characterization of polyphenol oxidase from Uapaca kirkiana fruit

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