Comparison of biochemical properties and thermal inactivation of membrane‐bound polyphenol oxidase from three apple cultivars (<i>Malus domestica</i> Borkh)

Liu, Fang; Han, Qianyun; Ni, Yingdong

doi:10.1111/ijfs.13676

Cited by 17 publications

(15 citation statements)

References 31 publications

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“…unicolor cotton PPO. These results are consistent with many previous studies, where Z-value for different PPOs usually ranges between 10 and 18°C (Benaceur et al, 2019;Liu et al, 2018; . The ΔS represents the reversibility of the transformation, the disorder, and/ or homogeneity degree of the system (Gouzi et al, 2012).…”

Section: Thermal Inactivationsupporting

confidence: 94%

“…Christoffersen (2016) also found two optimal pH values of 5.0 and 7.0 when studying avocado PPO. Coincidentally, two optimum pH levels were also founded in apple (Liu et al, 2018) and edible desert truffle (Gouzi, Depagne, Benmansour, & Coradin, 2013). This difference might be due to the two isoenzymes with different properties or the two ionization states of the substance generated from the enzyme and substrate reaction (Weemaes, Ludikhuyze, Van den Broeck, Hendrickx, & Tobback, 1998).…”

Section: Ph Optimum and Stabilitymentioning

confidence: 99%

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Comparison of the biochemical properties and thermal inactivation of polyphenol oxidase from three lily bulb cultivars

et al. 2020

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The biochemical properties and thermal inactivation of polyphenol oxidase (PPO) from three main planted lily cultivars in China, namely, Lilium lancifolium Thunb, Lilium brownie var. viridulum, and Lilium davidii var. unicolor cotton were evaluated. Data indicate that the PPO from three cultivars showed two optimum pH levels of 4.0 and 6.5-7.0 and temperature of 15°C and exhibited the highest affinity toward 4-methylcatechol. However, this enzyme did not exhibit monophenolase activity. Thiourea and L-cysteine were more effective than other inhibitors. The enzymatic activity of L. lancifolium Thunb PPO crude extract was higher than that of L. brownie var. viridulum and L. davidii var. unicolor cotton. For thermal inactivation, L. davidii var. unicolor cotton PPO showed the best thermal resistance at 65-75°C, and L. lancifolium Thunb showed stability at 45°C. The deactivation of the three types of PPO followed the first-order reaction kinetics, and the activation energy (E a) was 144.28, 138.00, and 107.12 kJ/mol for L. lancifolium Thunb PPO, L. brownie var. viridulum PPO, and L. davidii var. unicolor cotton PPO, respectively. Practical applications Lilium is an ornamental and edible plant typically used for food and traditional Chinese medicine. Its flowers are used for decoration, and its underground bulbs are rich in various bioactive substances. Fresh lily bulbs easily turn brown and lose economic value during storage and processing. Polyphenol oxidase (PPO) is a crucial molecule involved in the enzymatic browning of fruit and vegetables. In this study, PPO was extracted from three main planted lily cultivars in China. Namely, Lilium lancifolium Thunb, Lilium brownie var. viridulum, Lilium davidii var. unicolor cotton and was partially characterized. The results are of considerable importance to further understand the PPO of lily bulbs and provide guidance for the inactivation of enzymes and the processing of lily bulb juice.

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Section: Thermal Inactivationsupporting

confidence: 94%

Section: Ph Optimum and Stabilitymentioning

confidence: 99%

Comparison of the biochemical properties and thermal inactivation of polyphenol oxidase from three lily bulb cultivars

et al. 2020

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“…Similarly, PPO activity from blueberry was at 420 nm (Siddiq & Dolan, 2017;Terefe, Delon, Buckow, & Versteeg, 2015). The highest wavelength of absorbance at 410 nm was automatically assayed for PPO from Fuji apple (Fang, Zhao, Gan, & Ni, 2015) and at 412 nm was determined for Whangkeumbae pear (Zhou et al, 2018).…”

Section: Parameters For Measurement Of Ppomentioning

confidence: 99%

“…Therefore, enzymatic browning is believed to be one of the great challenges for vegetable and fruit industries (Anaya-Esparza et al, 2017;Sikora & Świeca, 2018). Several techniques including removing oxygen, heating, and high pressure have been regarded as useful measures to prevent enzymatic browning (Fang, Han, & Ni, 2017;Gavirangappa, Harshini, Arugakeerthy, Kulathooran, & Sr, 2018;Tinello & Lante, 2018). Moreover, the addition of inhibitors, which are non-toxic and highly active at low concentrations, is also an effective way to inhibit the browning reaction (Moon et al, 2018).…”

Section: Introductionmentioning

confidence: 99%

Purification and characterization of polyphenol oxidase (PPO) from water yam (Dioscorea alata)

Peng

et al. 2019

CyTA - Journal of Food

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Polyphenol oxidase (PPO) is responsible for the enzymatic browning of fruits and vegetables, and thus has negative effects on the quality of food. In this study, extraction and purification of PPO from water yam was performed successfully, and the characteristics of PPO and inhibitors of enzyme activity were analysed. The results showed that PPO activity improved by 4.58-fold through the DEAE-Sepharose and Superdex G-75 purification technique, which reached electrophoretic purity. The enzyme molecular weight was estimated to be 32 kDa. The optimum pH and temperature values of PPO were 6.0 and 35°C, respectively, and it was not thermostable at higher temperatures. PPO had the highest substrate affinity towards catechol (Km = 27.82 mmol/L and Vmax = 1.464 △A/ min). The most effective inhibitor was L-cysteine followed by ascorbic acid and sodium sulfite. Purificación y caracterización de la polifenol oxidasa (PPO) obtenida del ñame de agua (Dioscorea alata) RESUMEN La polifenol oxidasa (PPO) es responsable del pardeamiento enzimático de frutas y verduras; por lo tanto, tiene efectos negativos en la calidad de los alimentos. En el presente estudio se extrajo y se purificó con éxito la PPO proveniente del ñame de agua, y se analizaron sus características y los inhibidores de la actividad enzimática. En este sentido, los resultados indicaron que la actividad de la PPO mejoró 4.58 veces al emplear la técnica de purificación DEAE-Sepharose y Superdex G-75, que alcanzó la pureza electroforética. El peso molecular de la enzima se estimó en 32 kDa. Los valores óptimos de pH y temperatura de la PPO fueron 6.0 y 35°C, respectivamente, constatándose que no era termoestable a temperaturas más altas. La PPO mostró mayor afinidad de sustrato hacia el catecol (Km = 27.82 mmol/L y Vmax = 1.464 △A/min). Su inhibidor más efectivo fue la L-cisteína, seguida por el ácido ascórbico y el sulfito de sodio.

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“…This result shows that mPPO was more easily inactivated, compared with the released PPO. Previous studies demonstrated that the Fuji apple mPPO lost only 16.7% at 65 °C for 10 min (Liu et al ., ). The different results might due to the sufficient heating by RF treatment and higher treatment temperature.…”

Section: Resultsmentioning

confidence: 99%

Inactivation of apple (Malus domestica Borkh) polyphenol oxidases by radio frequency combined with pulsed electric field treatment

Tian

Wang

Yan

et al. 2018

Int J of Food Sci Tech

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Summary Radio frequency (RF) preprocessing combined with pulsed electric field (PEF) processing was employed to inactivate polyphenol oxidase (PPO) in apple juice. PPO enzyme levels, loss of total phenolic content (TPC), colours and volatile components in the apple juice were subsequently determined and compared with conventional processing methods (60 °C for 10 min and 70 °C for 10 min). Results indicated that, when the apple tissue was preprocessed using RF for 10 min, the residual activity of PPO decreased to 13.57%; when the squeezed juice was processed by PEF, the residual activity decreased to about 5% at 15–35 kV cm−1 for 400 μs. RF treatment caused no significant loss in TPC. Compared with the conventionally processed samples, the apple juice that was RF‐treated for 10 min and PEF‐treated at 15 kV cm−1 for 400 μs increased its lightness and maintained its fresh‐like flavour.

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Comparison of biochemical properties and thermal inactivation of membrane‐bound polyphenol oxidase from three apple cultivars (Malus domestica Borkh)

Cited by 17 publications

References 31 publications

Comparison of the biochemical properties and thermal inactivation of polyphenol oxidase from three lily bulb cultivars

Comparison of the biochemical properties and thermal inactivation of polyphenol oxidase from three lily bulb cultivars

Purification and characterization of polyphenol oxidase (PPO) from water yam (Dioscorea alata)

Inactivation of apple (Malus domestica Borkh) polyphenol oxidases by radio frequency combined with pulsed electric field treatment

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