Mechanism studies of gliadin-glucose glycation reaction and products formation by heat treatment with different conduction modes

Food Chem. 2024 Nov 19;465(Pt 2):142114. doi: 10.1016/j.foodchem.2024.142114. Online ahead of print.

Abstract

Heat treatments induce protein-reducing sugar glycation reactions easily, leading to protein structural transformations and advanced glycation end products generation. In this study, effects of four heat conduction modes (air, contact, vapour and liquid-conduction) on the spatial conformation and glycation products of gliadin-glucose system were evaluated. The results showed that gliadin tertiary structure expanded and exposed more hydrophobic sites in vapour-conduction, resulting in more glycation sites. Conversely, air-conduction promoted the protein folded, causing a lighter glycation degree and lower glyoxal, methylglyoxal, acrylamide, 5-hydroxymethylfurfural and carboxymethyl lysine contents (following vapour-conduction > contact-conduction > liquid-conduction > air-conduction). The above phenomena were attributed to the different water content in the different conduction modes. Furthermore, the glycation sites identified in vapour-conduction and contact-conduction were approximately two-fold of that in air-conduction. Conclusively, gliadin-glucose systems subjected to air-conduction showed less glycated intensity and hazardous products.

Keywords: Different conduction modes; Gliadin; Glycation product; Heat treatment.