Pectin methylesterase from kiwi and kaki fruits: Purification, characterization, and role of pH in the enzyme regulation and interaction with the kiwi proteinaceous inhibitor

被引：32

作者：

Ciardiello, MA

Tamburrini, M

Tuppo, L

Carratore, V

Giovane, A

Mattei, B

Camardella, L

机构：

[1] CNR, Inst Prot Biochem, I-80125 Naples, Italy

[2] Univ Naples 2, Dept Biochem & Biophys, I-80138 Naples, Italy

[3] Univ Roma La Sapienza, Dept Plant Biol, I-00185 Rome, Italy

来源：

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY | 2004年 / 52卷 / 25期

关键词：

pectin methylesterase; kiwi; kaki; salt and pH dependence of catalysis; protein-inhibitor interaction; surface plasmon resonance;

D O I：

10.1021/jf0491963

中图分类号：

S [农业科学];

学科分类号：

09 ;

摘要：

Pectin methylesterase was purified from kiwi (Actinidia chinensis) and kaki fruit (Diospyros kaki). The pH values of the fruit homogenates were 3.5 and 6.2, respectively. The kiwi enzyme is localized in the cell wall and has a neutral-alkaline pl, whereas the kaki enzyme is localized in the soluble fraction and has a neutral-acidic pl. The molecular weights of the kiwi and kaki enzymes were 50 and 37 kDa, respectively. The two enzymes showed a similar salt and pH dependence of activity, and a different pH dependence of the inhibition by the kiwi proteinaceous inhibitor.

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页码：7700 / 7703

页数：4

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