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KMID : 0624620110440010064
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BMB Reports
2011 Volume.44 No. 1 p.64 ~ p.69
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Purification and enzymatic properties of a peroxidase from leaves of Phytolacca dioica L. (Omb? tree)
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Guida Vincenzo
Criscuolo Giovanna
Tamburino Rachele
Malorni Livia
Parente Augusto
Di Maro Antimo
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Abstract
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A peroxidase (PD-cP; 0.47 mg/100 g leaves) was purified from autumn leaves of Phytolacca dioica L. and characterized. PD-cP was obtained by acid precipitation followed by gel-filtration and cation exchange chromatography. Amino acid composition and N-terminal sequence of PD-cP up to residue 15 were similar to that of Spinacia oleracea (N-terminal pairwise comparison showing four amino acid differences). PD-cP showed a molecular mass of approx. 36 kDa by SDS-PAGE, pH and temperature optima at 3.0 and 50.0°C, respectively and seasonal variation. The Michaelis-Menten constant (K(M)) for H(2)O(2) was 5.27 mM, and the velocity maximum (V(max)) 1.31 nmol min(-1), while the enzyme turnover was 0.148 s(-1). Finally, the presence of Ca(2+) and Mg(2+) enhanced the PD-cP activity, with Mg(2+) 1.4-fold more effective than Ca(2+).
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KEYWORD
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Enzymatic activity, Kinetics, Peroxidase, Phytolacca dioica, Protein purification
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