| Autor: |
Patrizia Rasmussen, Hanne Frøkiær, Pasquale Ferranti, Francesco Addeo, Francesco Bonomi, Stefania Iametti |
| Rok vydání: |
2002 |
| Předmět: |
|
| Zdroj: |
European Journal of Biochemistry. 269:1362-1372 |
| ISSN: |
0014-2956 |
| DOI: |
10.1046/j.1432-1033.2002.02769.x |
| Popis: |
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 β-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. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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