Peer-Reviewed Journal Details
Mandatory Fields
Li, M., Auty, M.A.E., Crowley, S.V.; Kelly, A.L., O'Mahony, J.A. and Brodkorb, A.
2019
September
Food Hydrocolloids
Self-association of bovine -casein as influenced by calcium chloride, buffer type and temperature
Published
WOS: 18 ()
Optional Fields
-casein Dairy proteins Protein aggregation
The aim of this study was to investigate the aggregation behaviour of a pure -casein (-CNpure) and a -casein concentrate (-CNconc) as a function of temperature, presence of CaCl2 and buffer type (pH 6.8). The particle size distribution and turbidity of -casein (-CN) solutions were measured by dynamic light-scattering (DLS) and UV/vis spectroscopy between 4 and 55C. Upon heating (455C), the particle size of both -CN solutions increased, indicating self-association via hydrophobic interactions. It was shown that the self-association of -CN increased with increasing -CN concentration and that -CNpure self-associated at significantly lower concentration than -CNconc. Both turbidity and particle size measurements showed that -CN had similar aggregation behaviour in water and imidazole buffer (pH 6.8) but differed in sodium phosphate buffer (pH 6.8), especially at higher ionic calcium concentrations. In addition, Fourier Transform Infrared (FTIR) spectroscopy revealed very little change in the secondary structure of -CN during heating (455C). The microstructure of -CN aggregates was monitored during heating from 10 to 55C, followed by cooling to 10C, using polarised light microscopy. Spherical and heterogeneous aggregates were observed when heated at temperatures above 37C, which were reversible upon cooling. This study confirmed that -CN undergoes self-associates on heating that reverses upon cooling, with the aggregation process being highly dependent on the purity of -CN, the solvent type and the presence of ionic calcium.
10.1016/j.foodhyd.2018.09.035
Grant Details