Purification and partial biochemical characterization of polyphenol oxidase from mango (Mangifera indica cv. Manila)

Gisela Palma-Orozco, Norma A. Marrufo-Hernández, José G. Sampedro, Hugo Nájera

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39 Scopus citations

Abstract

Polyphenol oxidase (PPO) is an enzyme widely distributed in the plant kingdom that has been detected in most fruits and vegetables. PPO was extracted and purified from Manila mango (Mangifera indica), and its biochemical properties were studied. PPO was purified 216-fold by hydrophobic interaction and ion exchange chromatography. PPO was purified to homogeneity, and the estimated PPO molecular weight (MW) by SDS-PAGE was ≈31.5 kDa. However, a MW of 65 kDa was determined by gel filtration, indicating a dimeric structure for the native PPO. The isolated PPO showed the highest affinity to pyrogallol (Km = 2.77 mM) followed by 4-methylcatechol (Km = 3.14 mM) and catechol (Km = 15.14 mM). The optimum pH for activity was 6.0. PPO was stable in the temperature range of 20-70 °C. PPO activity was completely inhibited by tropolone, ascorbic acid, sodium metabisulfite, and kojic acid at 0.1 mM.

Original languageEnglish
Pages (from-to)9832-9840
Number of pages9
JournalJournal of Agricultural and Food Chemistry
Volume62
Issue number40
DOIs
StatePublished - 8 Oct 2014

Keywords

  • Manila mango (Mangifera indica)
  • enzymatic browning
  • inhibitors
  • polyphenol oxidase
  • purification

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