| Attributs | Valeurs |
|---|
| type
| |
| Is Part Of
| |
| Subject
| |
| Title
| - Ability of αs-Casein to Suppress the Heat Aggregation ofOvotransferrin
|
| has manifestation of work
| |
| related by
| |
| Author
| |
| Abstract
| - The effects of αs-casein on heat aggregation of ovotransferrin (OT) were studied by heating at 80 °Cfor 20 min in 10 mM phosphate buffer, pH 7.0. The heat interactions between αs-casein and OTwere followed by turbidity development and polyacrylamide gel electrophoresis. We found that αs-casein can effectively suppress the heat-induced aggregation of heat-labile OT. The suppressiveability of αs-casein was reduced by the presence of NaCl on heating. Dephosphorylated αs-caseinhad less ability to suppress the aggregation of OT than native αs-casein. Our results indicate thatαs-casein interacts with the heat-denatured OT through its exposed hydrophobic surface andphosphoserine residue. Such interactions seem to be important in helping to suppress the aggregationof heated OT. The suppressive effects of αs-casein on heat aggregation of OT would be partiallyascribed to the formation of transparent gel from egg white by the addition of αs-casein. Keywords: αs-Casein; ovotransferrin; heat aggregation; dephosphorylation; ionic interaction; amphiphilic property
|
| article type
| |
| is part of this journal
| |
