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Polyphenol oxidase and enzymatic browning in apricot (Prunus armeniaca L.): Effect on phenolic composition and deduction of main substrates.


ABSTRACT: In this study, we investigate the effect of enzymatic browning on the phenolic composition of apricot in vivo and in vitro. The in vitro browning was caused by the recombinant latent apricot polyphenol oxidase (L-PaPPO). Successful heterologous expression of PaPPO in Escherichia coli yielded substantial amounts of enzyme containing both copper ions in the catalytic active site. The expressed L-PaPPO was characterized with regard to its molecular mass (56531.3 Da), pH optimum (7.0), activation by SDS, and enzyme kinetics. LC-MS/MS was used to compare the phenolic profiles of brown and non-brown apricots. The browning reactions did significantly decrease total phenolics and antioxidant capacity (measured with DPPH and CUPRAC assays). Catechin, epicatechin, and B-type procyanidins were the individual phenolics most affected by browning, followed by chlorogenic and neochlorogenic acid. These phenolics are most likely the main endogenous substrates of L-PaPPO, as they were oxidized much faster than the other identified phenolics.

SUBMITTER: Derardja AE 

PROVIDER: S-EPMC8789516 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature

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Polyphenol oxidase and enzymatic browning in apricot (<i>Prunus armeniaca</i> L.): Effect on phenolic composition and deduction of main substrates.

Derardja Ala Eddine AE   Pretzler Matthias M   Kampatsikas Ioannis I   Radovic Milena M   Fabisikova Anna A   Zehl Martin M   Barkat Malika M   Rompel Annette A  

Current research in food science 20220104


In this study, we investigate the effect of enzymatic browning on the phenolic composition of apricot <i>in vivo</i> and <i>in vitro</i>. The <i>in vitro</i> browning was caused by the recombinant latent apricot polyphenol oxidase (L-<i>Pa</i>PPO). Successful heterologous expression of <i>Pa</i>PPO in <i>Escherichia coli</i> yielded substantial amounts of enzyme containing both copper ions in the catalytic active site. The expressed L-<i>Pa</i>PPO was characterized with regard to its molecular m  ...[more]

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