Heat-induced amyloid-like aggregation of β-lactoglobulin regulated by glycation: A comparison of five kinds of reducing saccharides

Abstract The Maillard reaction occurs extensively in food industry and can change the aggregation behavior of dietary proteins. In this work, we reported the influence of glycation on the heat-induced amyloid-like aggregation behavior of β-lactoglobulin (β-Lg). Glycation was shown to accelerate the unfolding behavior of β-Lg and thereby increased fibrillation rate during initial heating according to 1-anilinonaphthalene-8-sulfonate and thioflavin T assays. Prolongation of fibrils was found to be limited by glycation derived from glucose, fructose and lactose, possibly due to the decrease in β-sheet structure of β-Lg based on circular dichroism spectral results and transmission electron microscopy images. β-Lg incubated with maltodextrin appeared to associate into globular micelles. Both covalent (disulfide bond and crosslinking structure) and non-covalent changes (steric hindrance and hydrogen bonds) induced by glycation are proposed to account for these fibrillation kinetic and conformational changes of β-Lg aggregates. According to these findings, glycation are promising methods to regulate both fibrillation kinetics and fibril conformation in the food industry.