Purification and characterization of pectin methylesterase from acerola (Malpighia glabra L.)
Contribuinte(s) |
Universidade Estadual Paulista (UNESP) |
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Data(s) |
20/05/2014
20/05/2014
15/08/2007
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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. |
Formato |
1845-1849 |
Identificador |
http://dx.doi.org/10.1002/jsfa.2884 Journal of the Science of Food and Agriculture. Chichester: John Wiley & Sons Ltd, v. 87, n. 10, p. 1845-1849, 2007. 0022-5142 http://hdl.handle.net/11449/38525 10.1002/jsfa.2884 WOS:000248240800008 |
Idioma(s) |
eng |
Publicador |
Wiley-Blackwell |
Relação |
Journal of the Science of Food and Agriculture |
Direitos |
closedAccess |
Palavras-Chave | #pectinmethylesterase #acerola #kinetic characterization #purification #isoenzymes #heat stability |
Tipo |
info:eu-repo/semantics/article |