title: Glucose slows down the heat-induced aggregation of β-lactoglobulin at neutral pH.
abstract: The behavior of β-lactoglobulin (β-Lg) during heat treatments depends on the environmental conditions. The influence of the presence or absence of a reducing sugar, namely, glucose, on the modification of the protein during heating has been studied using fluorescence, polyacrylamide gel electrophoresis (PAGE), size-exclusion chromatography (SEC), and transmission electron microscopy. Glycated products were formed during heating 24 h at 90 °C and pH 7. The fluorescence results revealed an accumulation of the advanced Maillard products and the formation of aggregates during heating. PAGE and SEC data suggested that the products in the control samples were essentially composed of covalently linked fibrillar aggregates and that their formation was faster than that for glycated samples. We showed that glucose affected the growing step of covalent aggregates but not the initial denaturation/aggregation step of native protein. Glucose-modified proteins formed a mixture of short fibrils and polydisperse aggregates. Our results revealed that β-Lg forms fibrils at neutral pH after heating and that glucose slows the formation of these fibrils.
authors: INRA, UMR1253 Science et Technologie du Lait et de l'Œuf, F-35042 Rennes, France.
authors: Michele
authors: M
authors: Da Silva Pinto
authors: Saïd
authors: S
authors: Bouhallab
authors: Antonio Fernandes
authors: AF
authors: De Carvalho
authors: Gwénaële
authors: G
authors: Henry
authors: Jean-Luc
authors: JL
authors: Putaux
authors: Joëlle
authors: J
authors: Leonil
mesh_terms: D005947:Glucose / Q000737:chemistry*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007782:Lactoglobulins / Q000737:chemistry*
chemical_list: D007782:Lactoglobulins; D005947:Glucose