American Chemical Society, Books and Journals Division
Journal of Agricultural and Food Chemistry vol:58 issue:19 pages:10761-10767
When gliadin, a mixture of wheat storage proteins containing only intramolecular disulfide (SS) bonds, is heated at high temperatures and preferably at alkaline pH, the SS bonds are cleaved by beta-elimination reactions leading to decreased cystine levels and the generation of dehydroalanine (DHA) and free sulfhydryl (SH) groups. DHA and the free SH group of cysteine can further react to form the irreversible' cross-link lanthionine (LAN). The kinetics of this reaction were studied by heating model systems containing gliadin at different pH values (pH 6.0, 8.0 and 11.0) at temperatures up to 120 degrees C. Multiresponse modeling was applied to simultaneously describe the course of the reaction partners, intermediates and products. The estimated kinetic parameters indicate that the reaction rate constant for the elimination reaction increases with temperature and pH. Moreover, the predominant reaction consuming the intermediary DHA is the cross-link with cysteine to form LAN following second-order reaction kinetics. The corresponding reaction rate constant is less dependent on temperature and pH. Use of the proposed kinetic model to estimate reaction product concentrations in cereal-based foods allowed us to conclude that the beta-elimination reaction may be less important during, e.g., bread making, but may well contribute to gluten network formation during the production of soft wheat products. It may also well be relevant in the production of bioplastics made from gluten.