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.
Pectin Methylesterase from Kiwi and Kaki Fruits: Purification, Characterization, and Role of pH in the Enzyme Regulation and Interaction with the Kiwi Proteinaceous Inhibitor / Ciardiello, M. A.; Tamburrini, M.; Tuppo, L.; Carratore, V.; Giovane, A.; Mattei, Maria Benedetta; Camardella, L.. - In: JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY. - ISSN 0021-8561. - STAMPA. - 52 (25):(2004), pp. 7700-7703. [10.1021/jf0491963]
Pectin Methylesterase from Kiwi and Kaki Fruits: Purification, Characterization, and Role of pH in the Enzyme Regulation and Interaction with the Kiwi Proteinaceous Inhibitor
MATTEI, Maria Benedetta;
2004
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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
