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Related Experiment Videos

Tomato peroxidase: purification, characterization, and catalytic properties.

D M Kokkinakis1, J L Brooks

  • 1Plant Science Division, College of Agriculture and Forestry, West Virginia University, Morgantown, West Virginia 26506.

Plant Physiology
|January 1, 1979
PubMed
Summary

Researchers purified a major tomato pericarp peroxidase, finding it similar to horseradish peroxidase (HRP) but with key differences in enzyme activity and subunit structure. This tomato peroxidase exhibits unique properties, including a distinct final form after dithiothreitol oxidation.

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Area of Science:

  • Plant biochemistry
  • Enzymology
  • Molecular biology

Background:

  • Peroxidases are crucial enzymes in plant physiology, involved in various metabolic processes.
  • Horseradish peroxidase (HRP) is a well-characterized plant peroxidase used extensively in research.
  • Understanding plant-specific peroxidases is essential for elucidating their roles in fruit development and ripening.

Purpose of the Study:

  • To isolate and characterize a major peroxidase from tomato pericarp (Lycopersicon esculentum var. Tropic).
  • To compare the biochemical and catalytic properties of the tomato peroxidase with those of horseradish peroxidase (HRP).
  • To investigate the structural differences between tomato peroxidase and HRP, particularly concerning subunit composition.

Main Methods:

  • Enzyme purification using a developed scheme to achieve approximately 85% purity.

Related Experiment Videos

  • Standard peroxidase assays to evaluate enzyme activity and kinetics.
  • Spectroscopic analysis to characterize enzyme intermediates and final forms.
  • Treatment with dithiothreitol to assess subunit dissociation and structural changes.

    • Main Results:

    • A major peroxidase was purified from ripe and green tomato pericarp.
    • Tomato peroxidase shares similarities with HRP in standard assays and intermediate complex formation (compounds I, II, and III).
    • Unlike HRP, tomato peroxidase does not catalyze the aerobic oxidation of indole-3-acetic acid under specific conditions.
    • Tomato peroxidase resolves into two nonidentical subunits upon dithiothreitol treatment, whereas HRP remains a single polypeptide.
    • During dithiothreitol oxidation, tomato peroxidase forms a unique 442 nm-absorbing species, unlike HRP.

    Conclusions:

    • Tomato pericarp contains a distinct peroxidase enzyme with unique catalytic and structural properties compared to HRP.
    • The observed differences in subunit structure and catalytic activity suggest specialized functions for tomato peroxidase in fruit physiology.
    • Further research into tomato peroxidase could reveal novel applications in biotechnology and plant science.