Isolation of a polyphenol oxidase (PPO) cDNA from artichoke and expression analysis in wounded artichoke heads

Plant Physiol Biochem. 2013 Jul:68:52-60. doi: 10.1016/j.plaphy.2013.03.020. Epub 2013 Apr 11.

Abstract

The polyphenol oxidase (PPO) enzyme, which can catalyze the oxidation of phenolics to quinones, has been reported to be involved in undesirable browning in many plant foods. This phenomenon is particularly severe in artichoke heads wounded during the manufacturing process. A full-length cDNA encoding for a putative polyphenol oxidase (designated as CsPPO) along with a 1432 bp sequence upstream of the starting ATG codon was characterized for the first time from [Cynara cardunculus var. scolymus (L.) Fiori]. The 1764 bp CsPPO sequence encodes a putative protein of 587 amino acids with a calculated molecular mass of 65,327 Da and an isoelectric point of 5.50. Analysis of the promoter region revealed the presence of cis-acting elements, some of which are putatively involved in the response to light and wounds. Expression analysis of the gene in wounded capitula indicated that CsPPO was significantly induced after 48 h, even though the browning process had started earlier. This suggests that the early browning event observed in artichoke heads was not directly related to de novo mRNA synthesis. Finally, we provide the complete gene sequence encoding for polyphenol oxidase and the upstream regulative region in artichoke.

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Catechol Oxidase / genetics*
  • Catechol Oxidase / metabolism
  • Cloning, Molecular
  • Cynara scolymus / enzymology
  • Cynara scolymus / genetics
  • Cynara scolymus / physiology*
  • DNA, Complementary
  • Gene Expression Regulation, Plant*
  • Light
  • Molecular Sequence Data
  • Molecular Weight
  • Phylogeny
  • Plant Proteins / genetics*
  • Plant Proteins / metabolism
  • Promoter Regions, Genetic

Substances

  • DNA, Complementary
  • Plant Proteins
  • Catechol Oxidase

Associated data

  • GENBANK/KC342809