Purification and characterization of pectin methylesterase from acerola (Malpighia glabra L.)

The enzyme pectinmethylesterase (PME) from acerola was extracted and purified by gel anion‐exchange chromatography (Q Sepharose) and filtration on Sephadex G‐100. The results showed two different PME isoforms (PME1 and PME2), with molecular masses of 25.10 and 5.20 kDa, respectively. PME1 specific activity increased by 9.63% after 60 min incubation at 98 °C, while PME2 retained 66% of its specific activity under the same conditions. The K m values of PME1, PME2 and concentrated PME were 0.94, 0.08 and 0.08 mg mL −1 , respectively. The V max value of PME1, PME2 and concentrated were 204.08, 2, 158.73 and 2.92 µmol min −1 mg −1 protein, respectively.