A previous study (Langmuir 2003, 19, 8436) used a Langmuir type pendant drop film balance to form beta-casein monolayers at the air-water interface. The present paper reports the application of that technique to the formation of protein monolayers at liquid interfaces. This technique allows a direct comparison between spread and adsorbed beta-casein interfacial behaviors that is presented in terms of their pi-A isotherms and static elasticity moduli. Pi-A isotherms of adsorbed and spread protein have been compared and found to be fairly similar in shape, stability, and also hysteresis phenomena. Examination of the elasticity moduli of both layers shows a similar analogy although slight differences arise and are interpreted in terms of the protein unfolding extent attained by both procedures at the oil interface.