1. Glucose slows down the heat-induced aggregation of b-lactoglobuline at neutral pH
- Author
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Joëlle Léonil, Antônio Fernandes de Carvalho, Jean-Luc Putaux, Michele da Silva Pinto, Gwénaële Henry, Saïd Bouhallab, Science et Technologie du Lait et de l'Oeuf (STLO), Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST, Laboratory of Research in milk products, Universidade Federal de Vicosa (UFV), Centre de Recherches sur les Macromolécules Végétales (CERMAV), Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA), Institut de Chimie Moléculaire de Grenoble, Université Joseph Fourier - Grenoble 1 (UJF), Capes (Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior, Brasil), FAPEMIG (Fundacao de Amparo a Pesquisa de Minas Gerais, Brasil), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), and Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Joseph Fourier - Grenoble 1 (UJF)
- Subjects
Hot Temperature ,chauffage ,Lactoglobulins ,02 engineering and technology ,Fibril ,beta-lactoglobuline ,symbols.namesake ,0404 agricultural biotechnology ,[SDV.IDA]Life Sciences [q-bio]/Food engineering ,Denaturation (biochemistry) ,glucose ,Polyacrylamide gel electrophoresis ,chemistry.chemical_classification ,Chromatography ,04 agricultural and veterinary sciences ,General Chemistry ,Hydrogen-Ion Concentration ,021001 nanoscience & nanotechnology ,040401 food science ,Fluorescence ,lait ,Reducing sugar ,Maillard reaction ,chemistry ,réaction de Maillard ,Transmission electron microscopy ,Covalent bond ,symbols ,0210 nano-technology ,General Agricultural and Biological Sciences ,accumulation - 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.
- Published
- 2012
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