Structural features of bovine caseinomacropeptide A and B by 1H nuclear magnetic resonance spectroscopy.

Abstract

Samples of bovine caseinomacropeptide (CMP) were isolated from kappa-casein A and kappa-casein B and fractionated to give aglycosylated CMP A and CMP B and monoglycosylated CMP A. The secondary structures of these three peptides were compared under neutral and acidic (pH 4.2) conditions, using two-dimensional (2D) 1H nuclear magnetic resonance (NMR) spectroscopy. The differences between the spectra at pH 4.2 and 7.0 and the spectra of the aglycosylated and glycosylated CMP A were subtle, indicating little change in backbone conformation with these changes. These results Suggest that differences in the coagulation properties of milks containing either kappa-casein A or kappa-casein B are more likely to be related to factors, such as micelle size or charge, than to structural differences arising from altered backbone conformation of the macropeptide segments of the kappa-caseins.