Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 69, Issue 50, Pages 15218-15230Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jafc.1c06043
Keywords
litchi; pericarp browning; laccase; polymerization; flavonoids; proanthocyanidins; HPLC-MS-MS
Funding
- National Natural Science Foundation of China [31772036, 32072638]
- Natural Science Foundation of Guangdong Province, China [2018B030311057]
- China Agriculture Research System of MOF [CARS-3215]
- China Agriculture Research System of MARA [CARS-3215]
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After harvest, litchi pericarp quickly turns brown, with decreases in (-)-epicatechin and procyanidins contents. The enzyme ADE/LAC plays a critical role in catalyzing the conversion of procyanidins, contributing to the browning process of the pericarp.
Litchi pericarp turns brown rapidly after fruit harvest, while the mechanism remains obscure. The contents of (-)-epicatechin (EC) and procyanidins (PCs) A2/B1/B2/C1 decreased during the pericarp browning, and a previously identified laccase (ADE/LAC) showed activity to these compounds, with brown products observed in the reactions. By UPLC-DAD-QTOF-MS/MS, isomers of dimeric, trimeric, and tetrameric PCs were detected in the EC-ADE/LAC reaction. In the presence of cyanidin-3-O-rutiside and rutin, anthocyanin-EC and rutin-EC adducts were, respectively, produced, and darker brown precipitation was observed in these reactions relatively to the EC-ADE/LAC reaction alone. ADE/LAC catalyzed the conversion of PC B2 to A-type PC dimers and B-type PC tetramers. ADE/LAC complemented the transparent testa of Arabidopsis LAC15-loss-of-function mutant (tt10) to wild-type dark brown seed coat. The results demonstrated that ADE/LAC-mediated flavonoid polymerization played an important role in the browning of pericarp.
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