Abstract
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.KeywordsDisulfide BondFood SafetySulfhydryl GroupSesquiterpene LactoneLima BeanThese 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.
Published Version
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call