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Purification and characterization of pectin methylesterase from acerola ( Malpighia glabra L.)
Author(s) -
de Assis Sandra Aparecida,
Martins Antônio Baldo Geraldo,
de Faria Oliveira Olga Maria Mascarenhas
Publication year - 2007
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2884
Subject(s) - chemistry , pectinesterase , pectin , size exclusion chromatography , sephadex , chromatography , enzyme , incubation , ion chromatography , biochemistry , pectinase
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. Copyright © 2007 Society of Chemical Industry