Competitive adsorption of protein at air-water or oil-water interfaces has received increasing attention, to improve the stability of foams and emulsions. In particular, systems combining globular and disordered flexible proteins have been studied broadly . Globular proteins are typically described as more rigid and require denaturation to adsorb at hydrophobic interfaces , or at least conformational changes underpinning surface adsorption and selfassociation . In turn, disordered proteins such as casein can adsorb faster at interfaces, owing to their softer, less structured architecture . This reflects the required energy of activation associated with denaturation and protein conformation typical of globular protein assembly, therefore modulating protein adsorption kinetics and regulating competitive adsorption profiles . In most cases, studies have focused on the interfacial composition and to some extent dilatational rheological properties of corresponding mixed assemblies, and few studies have investigated their interfacial shear mechanics.