The objective of this study was to investigate the impact of natural variations in aS1-casein and b-casein composition of milk on chymosin-induced hydrolysis of these caseins in milk gels and in sodium caseinate solutions. At 50% casein degradation, 15% more of aS1-casein with eight phosphate groups was hydrolysed compared with aS1-casein with nine phosphate groups in chymosin-induced milk gels. Furthermore, in sodium caseinate solutions, >10% more b-casein A2 was degraded compared with bcasein A1 and B at 50% casein degradation. Proteolysis by chymosin was not impacted by natural variation in the aS1-casein/b-casein ratio. Natural variation in aS1-casein/b-casein ratio did not impact upon firmness and gel strength in milk gels. Overall, comparison of sodium caseinate solutions to milk gels showed that differences in either phosphorylation of aS1-casein or amino acid composition of b-casein caused significant differences in degradation by chymosin, possibly due to changes in physical conformation of caseins.
- rennet coagulation properties
- bovine alpha-s1-casein
- secondary structure
- individual cows