Conformation of beta-Lactoglobulin at an Oil/Water Interface as Determined from Proteolysis and Spectroscopic Methods.
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.
Dufour
E
LEIMA, Institut National de la Recherche Agronomique, Nantes Cedex 03, 44316, France
Dalgalarrondo
M
Adam
L