A fraction derived from the membrane of milk fat globules (MFGM) was isolated from fresh raw cream. The adsorption of MFGM at the interface of oil-in-water emulsions was studied as well as the stability of the emulsions under different conditions (pH, temperature treatment) and the surface potential. The emulsions prepared with MFGM isolates were stable at neutral pH and were destabilized at low pH. By analysis of the protein adsorbed at the interface by polyacrylamide gel electrophoresis, we also determined that the MFGM that covered the surface of the oil-in-water emulsion could not be displaced by surfactants such as Tweens and Triton X-100 and was not affected by the presence of other proteins such as caseins and β-lactoglobulin added to the emulsion. A strong molecular interaction between the adsorbed MFGM, composed of phospholipid and protein, may exist at the interface, rendering the newly formed membrane very little affected by the presence of other surfactants. This MFGM-stabilized emulsion was characterized by a behaviour very different from that of emulsions stabilized by other milk proteins.