Isolation and Some Properties of an Acidic Fraction of Polyphenol Oxidase From Jerusalem Artichoke(helianthus Tuberosus L.)

Zawistowski, Jerzy; Βiliaderis, Costas G.; Murray, E.D.

doi:10.1111/j.1745-4514.1988.tb00134.x

Cited by 13 publications

(11 citation statements)

References 23 publications

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“…PPO is a copper-containing enzyme and widely distributed in plants (3). It has been studied in several plant tissues such as apples (4-7), bananas (8)(9)(10), peaches (11), grapes (12,13), kiwis (14), pears (15,16), raspberries (17), strawberries (18), plums (19), herbs (20), spinach (21), broad beans (22,23), field beans (24), wild potatoes (25), Jerusalem artichokes (26,27), cabbages (28), and tea leaves (29,30). The enzyme catalyzes two different reactions involving molecular oxygen.…”

Section: Introductionmentioning

confidence: 99%

Partial Purification of Polyphenol Oxidase from Chinese CabbageBrassica rapaL.

Nagai

Suzuki

2001

J. Agric. Food Chem.

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Polyphenol oxidase (PPO) was purified and characterized from Chinese cabbage by ammonium sulfate precipitation and DEAE-Toyopearl 650M column chromatography. Substrate staining of the crude protein extract showed the presence of three isozymic forms of this enzyme. The molecular weight of the purified enzyme was estimated to be approximately 65 kDa by gel filtration on Toyopearl HW-55F. On SDS-PAGE analysis, this enzyme was composed of a subunit molecular weight of 65 kDa. The optimum pH was 5.0, and this enzyme was stable at pH 6.0 but was unstable below pH 4.0 or above pH 7.0. The optimum temperature was 40 degrees C. Heat inactivation studies showed temperatures >40 degrees C resulted in loss of enzyme activity. PPO showed activity to catechol, pyrogallol, and dopamine (K(m) and V(max) values were 682.5 mM and 67.6 OD/min for catechol, 15.4 mM and 14.1 OD/min for pyrogallol, and 62.0 mM and 14.9 OD/min for dopamine, respectively). The most effective inhibitor was 2-mercaptoethanol, followed in decreasing order by ascorbic acid, glutathione, and L-cysteine. The enzyme activity of the preparation was maintained for 2 days at 4 degrees C but showed a sudden decreased after 3 days.

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Section: Introductionmentioning

confidence: 99%

Partial Purification of Polyphenol Oxidase from Chinese CabbageBrassica rapaL.

Nagai

Suzuki

2001

J. Agric. Food Chem.

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“…1992) and banana PPOs are stable at 70C for 30 min (Yang et al. 2000) and Jerusalem artichoke PPO is stable at 60C for 30 min (Zawistowski et al. 1988a,b).…”

Section: Resultsmentioning

confidence: 99%

Characterization of Polyphenoloxidase From Wild Pear (Pyrus Elaegrifolia)

Yerlitürk¹,

Arslan²,

Sinan

et al. 2008

J Food Biochemistry

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Wild pear polyphenoloxidase (PePPO) was extracted and purified using a Sepharose 4B‐l‐tyrosine‐p‐amino benzoic acid affinity column. Optimum conditions for pH, temperature and heat inactivation were determined. At the optimum pH and temperature, KM and Vmax values for PePPO with catechol and pyrogallol were determined. The Vmax/KM showed that PePPO has the greatest activity toward catechol. Optimum pH for PePPO was pH 6.0 using catechol as substrate. Optimum temperatures of PePPO for pyragallol and catechol were 65 and 35C, respectively. Enzyme activity decreased because of heat denaturation with increasing temperature. Inhibition of PePPO was investigated using p‐aminobenzoic acid, ethyleneglycol, l‐cysteine, l‐tyrosine, sodium azide, p‐aminobenzenesulfonamide, β‐mercaptoethanol and dithiothreitol and catechol as substrate. Competitive‐type inhibition was obtained with ethyleneglycol, l‐cysteine, l‐tyrosine, p‐aminobenzenesulfonamide and dithiothreitol. Uncompetitive inhibition was obtained with β‐mercaptoethanol, sodium azide and p‐aminobenzoic acid. These results show that the most effective inhibitor for PePPO was dithiothreitol and that the type of inhibition depended on the origin of PPO. PRACTICAL APPLICATIONS In this present work, the properties of polyphenoloxidase in Pyrus elaegrifolia, including optimum temperature, optimum pH, substrate specificity and response to inhibitors, were studied.

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“…Polyphenol oxidase was purifi ed from Jerusalem artichoke tubers and was found to be primarily an o-dihydroxyphenol oxidase with apparent K m values of 1.9, 3.5 and 3.9 mM for chlorogenic acid, 4-methylcatechol and catechol, respectively (Zawistowski et al 1988b ). An acidic fraction of polyphenol oxidase was isolated purifi ed from Jerusalem artichoke tubers (Zawistowski et al 1988a ). The pH optimum for its oxidation of chlorogenic acid, 4-methylcatechol and catechol was 6.0.…”

Section: Nutritive/medicinal Properties Tuber Nutrients/phytochemicalsmentioning

confidence: 99%

Helianthus tuberosus

Lim¹

2014

Edible Medicinal and Non Medicinal Plants

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Isolation and Some Properties of an Acidic Fraction of Polyphenol Oxidase From Jerusalem Artichoke(helianthus Tuberosus L.)

Cited by 13 publications

References 23 publications

Partial Purification of Polyphenol Oxidase from Chinese CabbageBrassica rapaL.

Partial Purification of Polyphenol Oxidase from Chinese CabbageBrassica rapaL.

Characterization of Polyphenoloxidase From Wild Pear (Pyrus Elaegrifolia)

Helianthus tuberosus

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