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.
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