The dynamic adsorption of the proteins at the oil–water interface was investigated with a
DSA100 Analyzer (Krüss, Hamburg, Germany) using the pendant drop method. In the process of measuring the dynamic surface pressure (π), a drop of 8 μL was automatically created by a software-controlled automatic dosing system after a 5 s stabilization. Droplet images were continuously viewed and captured using a video image acquisition system with a CCD camera, and then analyzed according to the Young–Laplace formula. The Ward–Tordai diffusion model was adopted to analyze the diffusion kinetics of proteins at the interface [23 (
link)]:
where
is the concentration of the initial protein solution,
is the Boltzmann constant,
is the absolute temperature, and
is the diffusion coefficient.
The surface dilatational properties were measured on a
DSA100 Analyzer (Krüss, Hamburg, Germany) using the EDM/ODM module. The amplitude and frequency were maintained at 0.2 and 0.1 Hz, respectively. The surface dilatational modulus, E, was acquired through analyzing the surface area change [24 (
link)].
Jiang J., Nie Y., Sun X, & Xiong Y.L. (2021). Partial Removal of Phenolics Coupled with Alkaline pH Shift Improves Canola Protein Interfacial Properties and Emulsion in In Vitro Digestibility. Foods, 10(6), 1283.