Purification and characterization of pectin methylesterase from acerola (Malpighia glabra L.)
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Data
2007-08-15
Autores
de Assis, Sandra Aparecida
Martins, Antonio Baldo Geraldo
de Faria Oliveira, Olga Maria Mascarenhas
Título da Revista
ISSN da Revista
Título de Volume
Editor
Wiley-Blackwell
Resumo
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. PMEI specific activity increased by 9.63% after 60 min incubation at 98 degrees C, while PME2 retained 66% of its specific activity under the same conditions. The K-m values of PMEI, PME2 and concentrated PME were 0.94, 0.08 and 0.08mg mL(-1), respectively. The V-max value of PMEI, PME2 and concentrated were 204.08, 2, 158.73 and 2.92 mu mol min(-1) mg(-1) protein, respectively. (c) 2007 Society of Chemical Industry.
Descrição
Palavras-chave
pectinmethylesterase, acerola, kinetic characterization, purification, isoenzymes, heat stability
Como citar
Journal of the Science of Food and Agriculture. Chichester: John Wiley & Sons Ltd, v. 87, n. 10, p. 1845-1849, 2007.