PMID: 38265Apr 1, 1979

Covalent bonds formed in proteins during milk sterilization: studies on caseins and casein peptides

The Journal of Dairy Research
D Lorient


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.


May 1, 1986·The Journal of Dairy Research·D W West
Dec 31, 1997·Critical Reviews in Food Science and Nutrition·G I ImafidonA M Spanier


Feb 1, 1976·The Journal of Dairy Research·D Lorient, G Linden
Jan 1, 1977·Advances in Experimental Medicine and Biology·M Sternberg, C Y Kim
Dec 5, 1975·Science·M SternbergF J Schwende
Jan 1, 1967·Biochimica Et Biophysica Acta·H S Murthy Venkitasubramanian
Mar 1, 1970·The British Journal of Nutrition·J Bjarnason, K J CARPENTER
Feb 21, 1967·Biochimica Et Biophysica Acta·K R Woods, K T Wang
Dec 1, 1960·The Biochemical Journal·K J CARPENTER

Related Concepts

Casein allergenic extract
Covalent Interaction
Plasma Protein Binding Capacity
Peptide Fragments
Urine Lysine Measurement
Organopyrophosphorus Compounds
Lysine Hydrochloride

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