Casanova H, Dickinson E
Procter Department of Food Science, University of Leeds, Leeds LS2 9JT, United Kingdom.
J Agric Food Chem. 1998 Jan 19;46(1):72-76. doi: 10.1021/jf970600q.
The influence of casein surface composition on the stability toward flocculation by sodium chloride has been investigated for oil-in-water emulsions (20 vol % oil, 1 wt % total protein) prepared with a mixture of alpha(s1)-casein + beta-casein. It has been observed that the poor salt stability of emulsions containing 100% alpha(s1)-casein is greatly enhanced by the replacement of about one-third of the alpha(s1)-casein by beta-casein. With around half of the adsorbed protein layer consisting of beta-casein, emulsions remain stable at ionic strengths of 2 M NaCl in the presence or absence of calcium ions (5 mM). At the point of droplet flocculation in these emulsions, most of the casein present is associated with the surface of the droplets. These results provide definitive evidence for the important influence of the compositional balance in sodium caseinate on the colloidal stability behavior of casein-based emulsions.
已针对用α(s1)-酪蛋白+β-酪蛋白混合物制备的水包油乳液（20体积%油，1重量%总蛋白），研究了酪蛋白表面组成对氯化钠引起的絮凝稳定性的影响。据观察，通过用β-酪蛋白替代约三分之一的α(s1)-酪蛋白，可大大提高含100%α(s1)-酪蛋白乳液较差的盐稳定性。当吸附蛋白层约一半由β-酪蛋白组成时，乳液在存在或不存在钙离子（5 mM）的情况下，在2 M NaCl的离子强度下仍保持稳定。在这些乳液的液滴絮凝点，存在的大部分酪蛋白与液滴表面相关。这些结果为酪蛋白酸钠组成平衡对酪蛋白基乳液胶体稳定性行为的重要影响提供了确凿证据。
