American Potato Journal

, Volume 47, Issue 12, pp 457–468 | Cite as

Study of hydrogen peroxide, potato enzymes and blackspot

  • M. L. Weaver
  • E. Hautala


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.


Catalase Catechol H202 Chlorogenic Acid Russet Burbank Potato 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


La proporcion de oxidación de tyrosina, p-cresol y catechol por un enzima de la papa disminuyo a medida que la concentración del H2O2 aumentó. En contraste, la proporción de oxidación del ácido clorogenico aumento en presencia del H2O2. Catalase bovinadestruyo el H2O2 y as previeno efectivamente la inhibición del H2O2 inducido o la acceleración de oxidación de los cuatro substratos por el enzima de la papa. Peroxidasa del rábano picante, en presencia de H2O2, no oxido el monofenol, pero si (oxido) ambos polifenoles. Se discute la posible asociación del H2O2, peroxidasa, y catalasa con la susceptibilidad a la mancha negra del tubérculo (black spot).


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Copyright information

© Springer 1970

Authors and Affiliations

  • M. L. Weaver
  • E. Hautala
    • 1
  1. 1.Western Regional Research Laboratory, Agricultural Research ServiceU.S. Department of AgricultureAlbany

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