Purification and Characterization of Latent Polyphenol Oxidase from Apricot (<i>Prunus armeniaca</i> L.)

Derardja, Ala eddine; Pretzler, Matthias; Kampatsikas, Ioannis; Barkat, Malika; Rompel, Annette

doi:10.1021/acs.jafc.7b03210

Cited by 74 publications

(66 citation statements)

References 61 publications

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“…The results were similar to those of apricot (Derardja et al, 2017) and lily bulbs (L. lancifolium Thunb) (Yang & Wang, 2008). The enzyme kinetic parameters were calculated by using the double TA B L E 3 Effect of various inhibitors on the activity of lily bulbs PPO using catechol as a substrate.…”

Section: Substrate Specificity and Enzyme Kineticssupporting

confidence: 61%

“…viridulum PPOs in the range of 55-75°C, and its inactivation curve is Derardja, Pretzler, Kampatsikas, Barkat, and Rompel (2017), who reported that apricot PPO loses more than 82% of its activity after 2 min of heat treatment at 70°C. The heat resistance of PPO varies with the reaction of enzymes with different substrates.…”

Section: Temperature 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: Substrate Specificity and Enzyme Kineticssupporting

confidence: 61%

Section: Temperature 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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“…RA gradually decreased to 81.46% at 45 °C and showed a more rapid decrease to 61.64% and 45.14% at 55 and at 65 °C respectively. PPO is present in numerous (mature, immature, latent and active forms) isoforms, and its increased activity at 25 °C (TP) may be due to the presence of latent PPO [ 15 , 26 ]. In comparison, the results of HPCD treated quince juice showed that the RA decreased to 78.26%, 69.55%, 59.45% and 34.18% with increased temperatures of 25, 35, 45 and 55 °C respectively.…”

Section: Resultsmentioning

confidence: 99%

Inactivation, Aggregation and Conformational Changes of Polyphenol Oxidase from Quince (Cydonia oblonga Miller) Juice Subjected to Thermal and High-Pressure Carbon Dioxide Treatment

et al. 2018

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Polyphenol oxidase (PPO) causes the browning reaction in fruits and vegetables and deteriorates the quality. Thermal treatment for enzyme inactivation may result in defects as opposed to high pressure CO2 (HPCD) processing. In this study, the changes in activity, dissociation, aggregation and conformation of purified PPO from thermal and HPCD treated juice were investigated. HPCD exhibited inactivation of PPO at 55–65 °C whereas thermal processing alone at the same temperature resulted in PPO still showing activity. Under thermal treatment at 25 and 65 °C, the browning degree was higher (0.39 and 0.24) than for HPCD-treated juice (0.23 and 0.12). Fluorescence and circular dichroism spectral results indicated that HPCD induced large decreases in intensities, revealing a rearrangement of the secondary structure and destruction of the native configuration of the PPO molecule. The particle size distribution (PSD) pattern revealed structural modification leading to initial dissociation and subsequent aggregation of PPO after HPCD treatment. Polyacrylamide gel electrophoresis (PAGE) analysis exhibited that molecular size of protein was 40 kDa. In conclusion, the HPCD method was found to be more effective than thermal treatment to inactivate PPO. Structural modifications provided better insights into the phenomena of activation and inactivation of PPO.

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“…Therefore,i tw as suspected that the proenzyme undergoes self-cleavage,s evering the C-terminal domain from the pro-enzyme.W erecently observed asimilar process in apricot PPO,where the enzyme was spontaneously activated upon prolonged storage. [20] Thea ssumed selfcleavage of MdPPO1 was confirmed by SDS-PAGEo fp roenzyme solutions incubated at 4 8 8Cfor 20 days,indicating the activation of the pro-enzyme into its separated active and C-terminal domains ( Figure S1;s ee the Supporting Information for experimental details). To exclude the possibility that the observed self-cleavage was caused by contaminations originating from the expression host E. coli,f resh MdPPO1 enzyme was incubated with lysate of E. coli,w hich did not infer any change to the cleavage of MdPPO1 ( Figure S2).…”

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confidence: 83%

A Peptide‐Induced Self‐Cleavage Reaction Initiates the Activation of Tyrosinase

et al. 2019

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The conversion of inactive pro‐polyphenol oxidases (pro‐PPOs) into the active enzyme results from the proteolytic cleavage of its C‐terminal domain. Herein, a peptide‐mediated cleavage process that activates pro‐ Md PPO1 ( Malus domestica ) is reported. Mass spectrometry, mutagenesis studies, and X‐ray crystal‐structure analysis of pro‐ Md PPO1 (1.35 Å) and two separated C‐terminal domains, one obtained upon self‐cleavage of pro‐ Md PPO1 and the other one produced independently, were applied to study the observed self‐cleavage. The sequence Lys 355–Val 370 located in the linker between the active and the C‐terminal domain is indispensable for the self‐cleavage. Partial introduction (Lys 352–Ala 360) of this peptide into the sequence of two other PPOs, Md PPO2 and aurone synthase ( Cg AUS1), triggered self‐cleavage in the resulting mutants. This is the first experimental proof of a self‐cleavage‐inducing peptide in PPOs, unveiling a new mode of activation for this enzyme class that is independent of any external protease.

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Purification and Characterization of Latent Polyphenol Oxidase from Apricot (Prunus armeniaca L.)

Cited by 74 publications

References 61 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

Inactivation, Aggregation and Conformational Changes of Polyphenol Oxidase from Quince (Cydonia oblonga Miller) Juice Subjected to Thermal and High-Pressure Carbon Dioxide Treatment

A Peptide‐Induced Self‐Cleavage Reaction Initiates the Activation of Tyrosinase

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