Amyloid-like aggregation of protein induced by of glycation in physiological condition has been widely studied in medical science,whereasamyloid aggregation behavior regulated by glycationduring thermal processing is less recognized.Carbonyl compounds were co-incubated withβ-lactoglobulin (β-Lac)at 100 ℃ and neutral pH to partly elucidate the effect on glycation on amyloid-like aggregation behavior and the underlying mechanism by using eircular dichroism (CD),amyloid dyes (Thioflavin T and Congo red),transmission electron microscopy (TEM),dynamic light scattering (DLS) and ANS fluorescence.Fine-stranded fibrillar structures were observed in TEM images of samples glycated with glucose (Glu) and diacetyl (DA),and this can be ascribed to dramatic decline in surface hydrophobicity which suppressedhydrophobic aggregation to a large extent.In addition,CDanalysisindicated significant adverse effect of glyoxal (GO) and methylglyoxal(MGO) derived glycation on the formation of β-sheet structure,resulting in their low capacity to form fibrils,as shown in ThT and CR binding essays.These resultssuggestamyloid aggregation of β-Lacduring thermal treatment could be regulated by restricting hydrophobic interaction as well as changing the secondary structure of theprotein during glycation.