Covalent bonds formed in proteins during milk sterilization: studies on caseins and casein peptides.
Formation of covalent bonds at milk sterilization temperatures was studied using caseins and casein peptides. At 120 degrees C lysinoalanyl residues produced even at pH 7.0 were derived from intra-molecular interactions between phosphoserine and lysine; the conditions of formation were determined. It was also found that the formation fo isopeptidic cross-links was significant with conditions more severe than those used for milk sterilization.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002364:Caseins; D002417:Cattle; D005511:Food Handling; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008239:Lysine; D008892:Milk; D009943:Organophosphorus Compounds / Q000032:analysis; D010446:Peptide Fragments; D011485:Protein Binding; D012694:Serine
D000596:Amino Acids; D002364:Caseins; D009943:Organophosphorus Compounds; D010446:Peptide Fragments; D012694:Serine; D008239:Lysine