Ability of alphas-Casein to suppress the heat aggregation of ovotransferrin.
The effects of alphas-casein on heat aggregation of ovotransferrin (OT) were studied by heating at 80 degrees C for 20 min in 10 mM phosphate buffer, pH 7.0. The heat interactions between alphas-casein and OT were followed by turbidity development and polyacrylamide gel electrophoresis. We found that alphas-casein can effectively suppress the heat-induced aggregation of heat-labile OT. The suppressive ability of alphas-casein was reduced by the presence of NaCl on heating. Dephosphorylated alphas-casein had less ability to suppress the aggregation of OT than native alphas-casein. Our results indicate that alphas-casein interacts with the heat-denatured OT through its exposed hydrophobic surface and phosphoserine residue. Such interactions seem to be important in helping to suppress the aggregation of heated OT. The suppressive effects of alphas-casein on heat aggregation of OT would be partially ascribed to the formation of transparent gel from egg white by the addition of alphas-casein.
Matsudomi
Naotoshi
N
Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University, Yamaguchi 753-8515, Japan. naotoshi@yamaguchi-u.ac.jp
Kanda
Yuka
Y
Yoshika
Youko
Y
Moriwaki
Hiromi
H
D002364:Caseins / Q000737:chemistry / Q000494:pharmacology*; D003207:Conalbumin / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D006358:Hot Temperature; D009391:Nephelometry and Turbidimetry; D010446:Peptide Fragments / Q000494:pharmacology; D010758:Phosphorus / Q000032:analysis; D010766:Phosphorylation; D012965:Sodium Chloride / Q000494:pharmacology
D002364:Caseins; D010446:Peptide Fragments; D003207:Conalbumin; D010758:Phosphorus; D012965:Sodium Chloride