Pectin methylesterase from kiwi and kaki fruits: purification, characterization, and role of pH in the enzyme regulation and interaction with the kiwi proteinaceous inhibitor |
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| Authors: | Ciardiello M Antonietta Tamburrini Maurizio Tuppo Lisa Carratore Vito Giovane Alfonso Mattei Benedetta Camardella Laura |
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| Institution: | Institute of Protein Biochemistry, CNR, Via Marconi 12, I-80125 Naples, Italy. ma.ciardiello@ibp.cnr.it |
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| Abstract: | 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 pI, whereas the kaki enzyme is localized in the soluble fraction and has a neutral-acidic pI. 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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