Characterization of a longan pericarp browning related peroxidase with a focus on its role in proanthocyanidin and lignin polymerization

The longan pericarp turns brown dramatically after harvesting, but the mechanism is not well understood. In this work, two peroxidases were purified from longan pericarp and found to be identical to the class III peroxidases PRX53-2 and PRX53-3. In vitro, PRX53-2/3 catalyzed the browning of several pericarp abundant proanthocyanidin and lignin monomers, such as (−)-epicatechin (EC), (+)-catechin (CT) and coniferyl alcohol (ConA). PRX53–2 was upregulated and highly-expressed, while PRX53-3 was expressed at low levels after harvesting; thus, PRX53-2 was considered a browning-related gene. The reaction with both proanthocyanidin and lignin presented a greater degree of brown coloration compared to the single substrate reactions. Several procyanidins isomers, EC-ConA and CT-ConA were detected in the double-substrate reaction. These results not only demonstrate that the effects of PRX53-2 on proanthocyanidin and lignin polymerization may be crucial for longan pericarp browning, but also help in developing new strategies or preservatives to delay pericarp browning. •PRX53-2/3 was purified from longan pericarp and showed high activity to guaiacol.•PRX53-2 is highly expressed during longan pericarp browning in postharvest storage.•PRX53-2 catalyzes proanthocyanidin and lignin monomers polymerization in vitro.•The polymerization of (epi)catechin is enhanced when ConA is present.•A new proposed mechanism helps in developing strategies to delay pericarp browning.