Sulfhydryl Groups and Food Safety

  • Mendel Friedman
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 177)


Sulfhydryl (thiol) compounds such as cysteine, N-acetylcysteine, and reduced glutathione interact with disulfide bonds of plant protease inhibitors via. sulfhydryl-disulfide interchange and oxidation reactions. Such interactions with inhibitors from soy and lima beans facilitate their heat inactivation of inhibitors, resulting in beneficial nutritional effects. Since thiols are potent nucleophiles, they have a strong avidity for unsaturated electrophilic centers of several dietary toxicants, including cyclopropene fatty acids, aflatoxins, sesquiterpene lactones, and trichothecenes. Such interactions may be used in vitro to lower the toxic potential of our food supply, and in vivo for prophylactic and therapeutic effects against antinutrients and food toxicants. A number of examples are cited to illustrate the concept of applying site-specific nucleophilic reagents such as thiols to reduce antinutritional and toxic manifestations of food ingredients by modifying pharmacophoric and toxicophoric electrophilic sites. Several related interactions between sulfhydryl groups and toxic compounds are also briefly mentioned to illustrate the generality of this approach.


Disulfide Bond Food Safety Sulfhydryl Group Sesquiterpene Lactone Lima Bean 
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Copyright information

© Plenum Press, New York 1984

Authors and Affiliations

  • Mendel Friedman
    • 1
  1. 1.Western Regional Research CenterARS-USDABerkeleyUSA

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