Purification and kinetic characterization of polyphenol oxidase from Barbados cherry (Malpighia glabra L.)
2008
Kumar, V.B Anil | Mohan, T.C Kishor | Murugan, K.
Polyphenol oxidase (PPO) of Barbados cherry was extracted and purified through ammonium sulfate precipitation, gel filtration, and affinity chromatography. The purification factor for PPO was 60% with 8.3% yield. The enzyme was characterized for thermal stability, pH and kinetic parameters. The molecular mass of PPO was approximately the sum of 52 and 38kDa estimated by SDS-PAGE. The purity was checked by native PAGE, showing a single prominent band. The optimum pH was 7.2. The enzyme had a temperature optimum at 40°C and was relatively stable at 60°C, with 55% loss of activity. Sodium diethyl dithiocarbamate (SDDC), l-cysteine and ascorbate significantly inhibited PPO activity. 4-Methyl catechol and catechol were found to be efficient diphenolic substrates for cherry PPO, considering the [formula removed] ratio. The data obtained in this study may help to understand cherry fruit browning.
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