Proteolysis of bovine β-lactoglobulin during thermal treatment in subdenaturing conditions highlights some structural features of the temperature-modified protein and yields fragments with low immunoreactivity
Research output: Contribution to journal › Journal article › Research › peer-review
Bovine β-lactoglobulin was hydrolyzed with trypsin or chymotrypsin in the course of heat treatment at 55, 60 and 65°C at neutral pH. At these temperatures β-lactoglobulin undergoes significant but reversible structural changes. In the conditions used in the present study, β-lactoglobulin was virtually insensitive to proteolysis by either enzyme at room temperature, but underwent extensive proteolysis when either protease was present during the heat treatment. High-temperature proteolysis occurs in a progressive manner. Mass spectrometry analysis of some large-sized breakdown intermediates formed in the early steps of hydrolysis indicated that both enzymes effectively hydrolyzed some regions of β-lactoglobulin that were transiently exposed during the physical treatments and that were not accessible in the native protein. The immunochemical properties of the products of βb-lactoglobulin hydrolysis were assessed by using various β-lactoglobulin-specific antibodies, and most epitopic sites were no longer present after attack of the partially unfolded protein by the two proteases.
Original language | English |
---|---|
Journal | European Journal of Biochemistry |
Volume | 269 |
Issue number | 5 |
Pages (from-to) | 1362-1372 |
Number of pages | 11 |
ISSN | 0014-2956 |
DOIs | |
Publication status | Published - 2002 |
- Bovine β-lactoglobulin, Limited proteolysis, Partial unfolding, Reduced immunoreactivity, Thermal treatment
Research areas
ID: 331794176