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

被引：15
|
作者：
de Assis, Sandra Aparecida
Martins, Antönio Baldo Geraldo
de Faria Oliveira, Olga Maria Mascarenhas
机构：
[1] UNESP, Dept Bioquim & Tecnol Quim, Inst Quim, BR-14801970 Araraquara, SP, Brazil
[2] Univ Estadual Feira de Santana, Dept Saude, BR-44031460 Feira De Santana, BA, Brazil
[3] UNESP, Dept Hort, Jaboticabal, SP, Brazil
来源：
JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE | 2007年 / 87卷 / 10期
关键词：
pectinmethylesterase; acerola; kinetic characterization; purification; isoenzymes; heat stability;
D O I：
10.1002/jsfa.2884
中图分类号：
S [农业科学];
学科分类号：
09 ;
摘要：
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.
引用
收藏
页码：1845 / 1849
页数：5
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