Study of hydrogen peroxide,potato enzymes and blackspot |
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Authors: | M. L. Weaver E. Hautala |
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Affiliation: | 1. Western Regional Research Laboratory, Agricultural Research Service, U.S. Department of Agriculture, 94710, Albany, California
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Abstract: | The rate of oxidation of tyrosine, p-cresol and catechol by potato enzyme diminished as H2O2 concentration increased. By contrast, the rate of oxidation of chlorogenic acid in the presence of H2O2 increased. Bovine catalase destroyed H2O2 and thus effectively prevented either H2O2-induced inhibition or acceleration of oxidation of the four substrates by potato enzyme. Horseradish peroxidase in the presence of H2O2 did not oxidize either monophenol, but oxidized both polyphenols. Possible association of H2O2, peroxidase and catalase with blackspot susceptibility is discussed. |
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