Rodríguez Patino J M, Rodríguez Niño M R, Sánchez C C
Departamento de Ingeniería Química, Universidad de Sevilla, Spain.
J Agric Food Chem. 1999 Jun;47(6):2241-8. doi: 10.1021/jf981119i.
In this paper we present surface dynamic properties (interfacial tension and surface dilational properties) of a whey protein isolate with a high content of beta-lactoglobulin (WPI) adsorbed on the oil-water interface as a function of adsorption time. The experiments were performed at constant temperature (20 degrees C), pH (5), and ionic strength (0.05 M). The surface rheological parameters and the interfacial tension were measured as a function of WPI concentration (ranging from 1 x 10(-)(1) to 1 x 10(-)(5)% w/w) and different processing factors (effect of convection and heat treatment). We found that the interfacial pressure, pi, and surface dilational modulus, E, increase and the phase angle, phi, decreases with time, theta, which should be associated with WPI adsorption. These phenomena have been related to diffusion of the protein toward the interface (at short adsorption time) and to the protein unfolding and/or protein-protein interactions (at long-term adsorption) as a function of protein concentration in solution and processing conditions.
在本文中,我们展示了一种富含β-乳球蛋白的乳清蛋白分离物(WPI)吸附在油水界面上时的表面动态特性(界面张力和表面扩张特性)与吸附时间的关系。实验在恒定温度(20摄氏度)、pH值(5)和离子强度(0.05M)下进行。测量了表面流变学参数和界面张力与WPI浓度(范围为1×10⁻¹至1×10⁻⁵% w/w)以及不同加工因素(对流和热处理的影响)的函数关系。我们发现,界面压力π和表面扩张模量E随时间θ增加,而相角φ随时间θ减小,这应该与WPI的吸附有关。这些现象与蛋白质向界面的扩散(在短吸附时间)以及蛋白质的展开和/或蛋白质-蛋白质相互作用(在长期吸附)有关,这是溶液中蛋白质浓度和加工条件的函数。