Acid-Induced Gelation of Caseins Glycated with Lactose: Impact of Maillard Reaction-Based Glycoconjugation and Protein Cross-Linking

During food processing or storage, milk proteins can react with reducing sugars via the Maillard reaction (glycation), which may alter their techno-functional properties. The aim of this study was to investigate the relationship between molecular changes of casein occurring during different stages of the Maillard reaction and its acid-induced gelling properties. Therefore, sodium caseinate was heated in a dry state at 60 °C in the presence of lactose and analyzed for structural modifications by determining Amadori compounds (glycoconjugation) indirectly as furosine, the total lysine modification, and the extent of protein cross-linking. For techno-functional characterization, acid-induced gels were prepared by the addition of glucono-δ-lactone and evaluated by measuring pH kinetics during gel formation, gel strength, and water holding capacity. The time to reach pH 4.6 during the gelation process was significantly delayed with increasing extent of the Maillard reaction. Glycation with lactose also led to a significant increase in gel strength and water holding capacity. The increase in gel stability was rather independent from the amount of sugars covalently bound to the proteins during the early phase of the Maillard reaction but strongly correlated to the degree of protein polymerization. Small- and medium-sized casein oligomers, formed during advanced stages of the Maillard reaction, contributed considerably to the formation of stronger gels with higher water holding capacity, whereas a sharp increase in the relative amount of the polymer fraction observed during prolonged cross-linking processes caused a spontaneous destabilization of the gel network. Knowledge about structure-function relationships on a molecular level can provide useful information to control food texture by raw material quality.