School of Food Science and Nutrition, University of Leeds, Leeds LS2 9JT, UK.
Colloids Surf B Biointerfaces. 2010 Nov 1;81(1):130-40. doi: 10.1016/j.colsurfb.2010.06.033. Epub 2010 Jul 7.
The flocculation properties of oil-in-water emulsions stabilized by proteins are reviewed from the colloid science perspective. Emphasis is placed on insight from systematic studies of the stability of emulsions prepared with a milk protein ingredient as the sole emulsifying agent. The main factors considered are pH, ionic strength, calcium ion concentration, thermal processing, and the presence of cosolutes (alcohol, sugars). Contrasting dependences of the flocculation behaviour on these factors are observed for the pH-sensitive disordered caseins (alpha(s1)-casein or beta-casein) and the heat-sensitive globular proteins (especially beta-lactoglobulin). In comparing characteristic emulsion properties obtained with different proteins, we consider the relative importance of the different kinds of molecular and colloidal interactions-electrostatic, steric, hydrophobic and covalent.
本文从胶体科学的角度综述了由蛋白质稳定的油包水乳状液的絮凝性质。重点介绍了利用乳蛋白作为唯一乳化剂制备乳液的稳定性的系统研究获得的深入见解。主要考虑的因素有 pH 值、离子强度、钙离子浓度、热处理和共溶剂(醇、糖)的存在。对于 pH 敏感的无规卷曲的酪蛋白(α(s1)-酪蛋白或β-酪蛋白)和热敏感的球状蛋白(特别是β-乳球蛋白),观察到絮凝行为对这些因素的依赖存在显著差异。在比较不同蛋白质获得的特征乳液性质时,我们考虑了不同种类的分子和胶体相互作用(静电、空间、疏水和共价)的相对重要性。