Peroxidase of Kiwifruit

Préstamo, Guadalupe

doi:10.1111/j.1365-2621.1989.tb04701.x

Cited by 14 publications

(4 citation statements)

References 7 publications

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“…4b), where the molecular weight of POII had the same value. This value is similar to the molecular weight value of buck wheat peroxidase (56,100 kDa) [23] and higher than those reported for peroxidases from papaya fruit (41-54 kDa) [24], oranges (22 to 44 kDa) [8], kiwi fruit (40-42 kDa) [25], pea nuts (40-42 kDa) [26], horse radish (44 kDa) [27] and Withania somnifera (34-48 kDa) [28]. The highest molecular weight was detected for marula fruit peroxidase (71 kDa) [29].…”

Section: Resultssupporting

confidence: 82%

Properties of a Cationic Peroxidase from Citrus jambhiri cv. Adalia

Mohamed

El-Badry

Drees

et al. 2008

Appl Biochem Biotechnol

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The major pool of peroxidase activity is present in the peel of some Egyptian citrus species and cultivars compared to the juice and pulp. Citrus jambhiri cv. Adalia had the highest peroxidase activity among the examined species. Four anionic and one cationic peroxidase isoenzymes from C. jambhiri were detected using the purification procedure including ammonium sulfate precipitation, chromatography on diethylaminoethanol-cellulose, carboxymethyl-cellulose, and Sephacryl S-200 columns. Cationic peroxidase POII is proved to be pure, and its molecular weight was 56 kDa. A study of substrate specificity identified the physiological role of POII, which catalyzed the oxidation of some phenolic substrates in the order of o-phenylenediamine > guaiacol > o-dianisidine > pyrogallol > catechol. The kinetic parameters (K (m), V (max), and V (max)/K (m)) of POII for hydrolysis toward H2O2 and electron donor substrates were studied. The enzyme had pH and temperature optima at 5.5 and 40 degrees C, respectively. POII was stable at 10-40 degrees C and unstable above 50 degrees C. The thermal inactivation profile of POII is biphasic and characterized by a rapid decline in activity on exposure to heat. The most of POII activity (70-80%) was lost at 50, 60, and 70 degrees C after 15, 10, and 5 min of incubation, respectively. Most of the examined metal ions had a very slight effect on POII except of Li+, Zn2+, and Hg2+, which had partial inhibitory effects. In the present study, the instability of peroxidase above 50 degrees C makes the high temperature short time treatment very efficient for the inactivation of peel peroxidase contaminated in orange juice to avoid the formation of off-flavors.

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Section: Resultssupporting

confidence: 82%

Properties of a Cationic Peroxidase from Citrus jambhiri cv. Adalia

Mohamed

El-Badry

Drees

et al. 2008

Appl Biochem Biotechnol

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“…. (Smith and Hammerschmidt 1988) and those of most fruits and vegetables (Vamos-Vigyazo 1981;Prestamo 1989;Padiglia and others 1995b;Civello and others 1995). A similar stain for the IEF gel, however, indicates 6 acidic peroxidase isozymes (Figure 3).…”

Section: Resultsmentioning

confidence: 98%

Effects of Ascorbic Acid on Peroxidase and Polyphenoloxidase Activities in Fresh‐Cut Cantaloupe Melon

And

Watson

2001

Journal of Food Science

119

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Peroxidase (POD) and polyphenol oxidase (PPO) in minimally processed cantaloupe melon (Cucumis melo L. var. reticulatus Naud) were assayed and the effect of ascorbic acid on their respective activities during storage at 4 Њ Њ Њ Њ ЊC was determined. POD activity decreased with storage and was inhibited by ascorbate treatment. Two native electrophoretic POD bands with estimated molecular weights 240 and 170 kDa respectively were obtained. Isoelectric focusing separated six acidic POD isozymes with isoelectric points between 5.1 and 6.0, possibly subunits of the POD isozymes. PPO activity in the cantaloupe melon extract was very weak and the fruit's content of oxidizable phenolic compounds was negligible.

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“…Determination of peroxidase activity: POD activity was assayed using a modifi cation of the spectrophotometric method of Rastogi et al (1999) and Préstamo (1989). The sample cuvette contained 80 μl enzyme extract and a mixture composed of 2.6 ml potassium phosphate buffer (10 mM, pH 6.0) with 0.1 ml (1%, w/v) p-phenylenediamine as H-donor and 0.2 ml (0.3%, v/v) hydrogen peroxidase as…”

Section: Methodsmentioning

confidence: 99%

Kinetic study of thermal inactivation of potato peroxidase during high-temperature short-time processing

Jin

Deng

et al. 2010

J Food Sci Technol

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Thermal inactivation curves for peroxidase in potato extracts were determined in the range of 100 to 140°C for 10 to 100 sec. The capillary tube method was used to obtain isothermal conditions. The come-up time for the capillary tubes was accurately calculated by analysis method by which thermal inactivation kinetics of enzymes in relation to high temperature processing would be more easily detected. Heat inactivation of potato peroxidase followed first-order reaction kinetics and yielded a curved Arrhenius plot for the temperature dependence at high temperatures. Kinetics parameters, k and Ea, were calculated for potato peroxidase. At temperature range of 100-140°C, the activation energy of peroxidase was lower than that in the range of 78-84°C. It could be elucidated by the scheme of thermal inactivation pathway.

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Peroxidase of Kiwifruit

Cited by 14 publications

References 7 publications

Properties of a Cationic Peroxidase from Citrus jambhiri cv. Adalia

Properties of a Cationic Peroxidase from Citrus jambhiri cv. Adalia

Effects of Ascorbic Acid on Peroxidase and Polyphenoloxidase Activities in Fresh‐Cut Cantaloupe Melon

Kinetic study of thermal inactivation of potato peroxidase during high-temperature short-time processing

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