Abstract
Pectin methylesterase (PME) (EC 3.1.1.11) has been purified to apparent homogeneity from ripe papaya fruits. The purification protocol consisted of ammonium sulphate precipitation (60-80%) and cation exchange chromatography in CM Sepharose CL-6B and Mono S. Papaya PME consists of two components (PME 1 and PME 2), which have been shown to be isoenzymes by Ferguson plot analysis. The molecular weight of the enzyme is 27,000 while its isoelectric point is greater than pH 9.0. The N-terminal sequences of PME 1 and PME 2 are SVVTPNAVVADDGVFXFKTG. Both PME 1 and PME 2 showed optimum activities at pH 8.0 and 35°C. The average K m s of PME 1 and PME 2 are 0.0071 and 0.0166 g/liter pectin respectively, while the corresponding average V maxs are 741 and 800 μmol methanol/min/mg protein, respectively. Papaya pectin methylesterase is activated by cations, but the effect is more pronounced for divalent than monovalent cations. Inhibition studies showed that sucrose is a noncompetitive inhibitor while p-chloromercuribenzoic acid has no significant effect on its activity.
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