Abstract
SummaryA recently described nuclear magnetic resonance (NMR) method was evaluated for its usefulness in studying thermal effects on milk proteins. The increase in water proton T2 relaxation rate observed during thermal treatment of aqueous whey protein solutions above the denaturing onset temperature paralleled results obtained with the standard Rowland (1938) method. The influence of milk constituants on NMR characteristics was analysed. The NMR response increased with the ionic strength and the addition of caseinate or casein micelles. The relevance of the T2 relaxation probe for studying thermal modifications of milk proteins is discussed. It is proposed to apply the NMR method for determining either reversible or irreversible thermal denaturation of whey proteins in model Systems.
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