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Purification, characterization and catalytic activity of anionic zucchini peroxidase

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Abstract

The isolation and purification, by preparative electrofocusing, of the major anionic (ZPOA) and cationic (ZPOC) isoenzymes, collected from young zucchini squash, are reported. The M r and sugar content are similar to those found previously for the major isoenzymes from the ripe fruits and in the range commonly observed for plant peroxidases. The amount of the two cationic enzymes was very low compared with that of anionic ZPOA. The anionic enzyme has been characterized by electronic, circular dichroism, proton NMR and electron paramagnetic resonance spectroscopy. The spectra are qualitatively similar to those of the corresponding anionic horseradish peroxidase (HRPA) derivatives, with minor differences attributable to the particular protein environment around the heme. The kinetics of the enzymatic oxidation of a series of phenols by H2O2 have been studied. ZPOA shows a parallel behavior to HRPA, but it is systematically more active than HRPA, indicating that the zucchini enzymes have a marked tendency to carry out oxidation of this type of compounds.

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Authors and Affiliations

  1. Dipartimento di Chimica Generale, Università di Pavia, Pavia, Italy

    Luigi Casella

  2. Dipartimento di Chimica Inorganica e Metallorganica, Università di Milano, Milano, Italy

    Michele Gullotti & Sonia Poli

  3. Dipartimento di Chimica Inorganica, Chimica Fisica e Chimica dei Materiali, Università di Torino, Torino, Italy

    Rosa Pia Ferrari & Enzo Laurenti

  4. Istituto per la nutrizione delle piante, Torino, Italy

    Augusto Marchesini

Authors
  1. Luigi Casella
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  2. Michele Gullotti
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  3. Sonia Poli
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  4. Rosa Pia Ferrari
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  5. Enzo Laurenti
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  6. Augusto Marchesini
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Casella, L., Gullotti, M., Poli, S. et al. Purification, characterization and catalytic activity of anionic zucchini peroxidase. Biometals 6, 213–222 (1993). https://doi.org/10.1007/BF00187758

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  • DOI: https://doi.org/10.1007/BF00187758

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