Abstract
AbstractSeveral food proteins were examined for their capacity as substrate in transglutaminase reaction by using a fluorescent amine, monodansyl cadaverine, as donor substrate and following the increase in fluorescence of the reaction mixture. Wheat gluten, or one of its component proteins, gliadin, was the best acceptor among the proteins tested. Compared with intact protein, a preparation of wheat gliadin, modified by transglutaminase‐mediated incorporation of [14C]lysine, showed a marked decrease in in‐vitro digestibility. In rat feeding tests, however, the luminal leavings and excreta collected 24 h after administration of gliadin with ϵ‐attached [14C]lysine contained less than one‐tenth of the radioactivity originally administered. The results presented support the previous notion that occurrence of the ϵ‐γ isopeptide linkage in protein does not significantly impair the in‐vivo digestibility of the protein and nutritional availability of isopeptide bound lysine moieties.
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 callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
