Huppertz Thom, de Kruif Cornelis G
Department of Food and Nutritional Sciences, University College Cork, Cork, Ireland.
J Dairy Res. 2007 May;74(2):194-7. doi: 10.1017/S0022029906002263. Epub 2007 Feb 12.
In the study presented in this article, the influence of added alpha-lactalbumin and beta-lactoglobulin on the changes that occur in casein micelles at 250 and 300 MPa were investigated by in-situ measurement of light transmission. Light transmission of a serum protein-free casein micelle suspension initially increased with increasing treatment time, indicating disruption of micelles, but prolonged holding of micelles at high pressure partially reversed HP-induced increases in light transmission, suggesting reformation of micellar particles of colloidal dimensions. The presence of alpha-la and/or beta-lg did not influence the rate and extent of micellar disruption and the rate and extent of reformation of casein particles. These data indicate that reformation of casein particles during prolonged HP treatment occurs as a result of a solvent-mediated association of the micellar fragments. During the final stages of reformation, kappa-casein, with or without denatured whey proteins attached, associates on the surface of the reformed particle to provide steric stabilisation.
在本文所介绍的研究中，通过原位测量光透射率，研究了添加α-乳白蛋白和β-乳球蛋白对酪蛋白胶束在250和300兆帕压力下所发生变化的影响。无血清蛋白的酪蛋白胶束悬浮液的光透射率最初随处理时间的增加而升高，表明胶束被破坏，但在高压下长时间保持胶束会部分逆转高压诱导的光透射率增加，这表明形成了胶体尺寸的胶束颗粒。α-乳白蛋白和/或β-乳球蛋白的存在并不影响胶束破坏的速率和程度以及酪蛋白颗粒重新形成的速率和程度。这些数据表明，在长时间高压处理过程中酪蛋白颗粒的重新形成是胶束片段通过溶剂介导缔合的结果。在重新形成的最后阶段，附着或未附着变性乳清蛋白的κ-酪蛋白在重新形成颗粒的表面缔合，以提供空间稳定作用。
