Effects of Glycated Glutenin Heat-Processing Conditions on Its Digestibility and Induced Inflammation Levels in Cells

Abstract

Protein is one of the three major macronutrients and is essential for health. The reaction of α-dicarbonyl compounds (α-DCs) with glutenin during heat processing can modify its structure, thereby reducing its digestibility. Furthermore, advanced glycation end products (AGEs) formed by the Maillard reaction are associated with long-term diabetes-related complications. In this study, we established a heat processing reaction system for α-DCs and glutenin by simulating common food processing conditions. An in vitro digestion model was used to study the digestibility of glycated glutenin; whereupon the effects of the digestion products on macrophage inflammatory response were further investigated. It was found that reaction conditions, including temperature, treatment duration, pH, and reactant mass ratio, can significantly affect the digestibility of glycation glutenin, in which the mass ratio of reactants has the most significant influence. We demonstrated that when the mass ratio of glutenin to methylglyoxal (MGO) was 1:3, the level of inflammation induced by glycated glutenin was the highest. The mass ratio of reactants significantly affects the digestibility of glycation glutenin and the level of macrophage-induced inflammatory response. This suggests that it is possible to protect the nutritional value of protein and improve food safety by controlling the heat processing conditions of wheat products.