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Title: Conformation of beta-Lactoglobulin at an Oil/Water Interface as Determined from Proteolysis and Spectroscopic Methods. Author: Dufour E, Dalgalarrondo M, Adam L. Journal: J Colloid Interface Sci; 1998 Nov 15; 207(2):264-272. PubMed ID: 9792769. Abstract: The rates of appearance of tryptic peptides following the hydrolysis of beta-lactoglobulin in solution or adsorbed at the oil/water interface of an emulsion were investigated as a function of time. It was also shown using hydrophobic labeling that the region 15-40 of beta-lactoglobulin was in the oil phase. The fluorescence results suggested that the conformation of beta-lactoglobulin was modified upon adsorption at the oil/water interface and that at least one tryptophan in adsorbed beta-lactoglobulin was in a more hydrophobic environment. The data obtained by circular dichroism in the peptidic region indicated that the adsorbed beta-lactoglobulin was characterized by a higher content in alpha-helix than the protein in solution. Copyright 1998 Academic Press.[Abstract] [Full Text] [Related] [New Search]