Purification and characterization of pectin methylesterase from acerola (Malpighia glabra L.)
Copyright policy )Purification and characterization of pectin methylesterase from acerola (Malpighia glabra L.)
AbstractThe 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 Km values of PME1, PME2 and concentrated PME were 0.94, 0.08 and 0.08 mg mL−1, respectively. The Vmax value of PME1, PME2 and concentrated were 204.08, 2, 158.73 and 2.92 µmol min−1 mg−1 protein, respectively. Copyright © 2007 Society of Chemical Industry
isoenzymes, purification, heat stability, pectinmethylesterase, kinetic characterization, acerola
isoenzymes, purification, heat stability, pectinmethylesterase, kinetic characterization, acerola
selected citations These citations are derived from selected sources.This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).15 popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.Average influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).Top 10% impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.Average
Citations provided by BIP!Popularity provided by BIP!