Heat treatment of β-lactoglobulin affects its digestion and translocation in the upper digestive tract.

Heat treatment is a commonly applied unit operation in the processing of β-lactoglobulin containing products. This does, however, influence its structure and thereby impacts its activity and digestibility. We describe how various heat-treatments of β-lactoglobulin change the digestibility using a modified version of the current consensus INFOGEST protocol. Additionally, protein was investigated for its translocation over the intestinal epithelial barrier, which would bring them in contact with immune cells. The extent of gastric digestibility was higher when the protein structure was more modified, while the influence of glycation with lactose was limited. Translocation studies of protein across Caco-2 cell monolayers showed a lower translocation rate of protein heated in solution compared to the others. Our study indicates that structural modifications after different heat-treatments of β-lactoglobulin increase in particular gastric digestibility and the translocation efficiency across intestinal epithelial cells.