Conformation of β-Lactoglobulin at an Oil/Water Interface as Determined from Proteolysis and Spectroscopic Methods
✍ Scribed by E. Dufour; M. Dalgalarrondo; L. Adam
- Publisher
- Elsevier Science
- Year
- 1998
- Tongue
- English
- Weight
- 153 KB
- Volume
- 207
- Category
- Article
- ISSN
- 0021-9797
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✦ Synopsis
The rates of appearance of tryptic peptides following the hydrolysis of -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 -lactoglobulin was in the oil phase. The fluorescence results suggested that the conformation of -lactoglobulin was modified upon adsorption at the oil/water interface and that at least one tryptophan in adsorbed -lactoglobulin was in a more hydrophobic environment. The data obtained by circular dichroism in the peptidic region indicated that the adsorbed -lactoglobulin was characterized by a higher content in ␣-helix than the protein in solution.