Abstract:The contact angles of protein Newton black foam films from ALG (alpha-lactalbumin), BLG (beta-lactoglobulin) and BSA (bovine serum albumin) are measured here within. The measurements are carried out under dynamic and equilibrium conditions. For all proteins, a strong hystheresis effect of the contact angle is observed under dynamic conditions. An attempt is made to explain these results by the slow adsorption and desorption kinetics of the protein bilayers and by the dynamic structure and the rheology of the protein network forming the bubble walls. In addition, we propose a modification of the experimental device reported previously for contact angle measurements of large flat films in equilibrium. The advantages of this method are discussed in detail. Some shortcomings (precision, reproducibility) of this preliminary variant of the device in this initial stage of its application, do not allow one to draw reliable conclusions about the interactions of these films. Some improvements of the measurement quality are proposed.