Function of parvalbumin from fish muscle in adsorption on the oil-water interface during emulsification.

在pH 7.0的条件下，用分散剂或超声波对鲤鱼肌肌浆蛋白（SP）和小白蛋白（PA）水溶液进行乳化，研究了两种蛋白在油水界面上的吸附行为和PA对乳液的稳定作用。激光衍射法、显微法和浊度法三种乳状液颗粒稳定性评价方法对pa -乳状液的稳定性评价趋势基本一致，而sp -乳状液的稳定性评价方法由于絮凝作用的存在存在一定差异。聚丙烯酸乳液粒径分布较好，粒径较小。在中性pH下，乳剂的不稳定性主要是由成乳引起的，不伴有絮凝和聚并。乳化液的絮凝和成乳分别与分子电荷和吸附蛋白的量密切相关。乳化过程中未观察到SP组分在油水界面上对PA的明显吸附。对于pa乳液，薄吸附在乳液颗粒上的带负电荷分子的静电斥力会增加乳液的稳定性。相反，由于乳状液颗粒的比重较小，这种薄的PA膜应该成为更快形成乳状液的一个因素，因此，微分散可以参与乳状液的稳定。

Aqueous solution of sarcoplasmic proteins (SP) and parvalbumin (PA) from carp muscle were emulsified with triolein at pH 7.0 using a disperser or a sonicator and the adsorption behavior of the proteins on the oil-water interface and the function of PA in stabilization of the emulsion were investigated.Three kinds of evaluation methods (laser diffractometry, microscopy and turbidimetry) for stability of emulsion particles showed almost identical tendency for PA-emulsions, while the values for SP-emulsion were somewhat discrepant among those methods because of the flocculation.PA-emulsion had a superior size distribution with smaller particles. Instability of the emulsions at neutral pH was mainly induced with creaming, not accompanied by flocculation nor coalescence. Flocculation and creaming of emulsion were closely associated with molecular charge and amount of adsorbed proteins, respectively. Predominant adsorption of PA among SP components on the oil-water interface was not observed during emulsification.For PA-emulsions the electrostatic repulsion by the negatively charged molecules thinly adsorbed on the emulsion particles should increase the emulsion stability. In contrast such a thin membrane of PA should become to be a factor of the faster creaming for the smaller specific gravity of the emulsion particles and, consequently, microdispersion could be involved in the emulsion stabilization.