Hydrophobins are proteins isolated from filamentous fungi, which are excellent foam stabilizers, unlike most of the proteins. In the present study, we demonstrate that hydrophobin HFBII can also serve as excellent emulsion stabilizer. The HFBII adsorption layers at the oil/water interface solidify similarly to those at the air/water interface. The thinning of aqueous films sandwiched between two oil phases ends with the formation of a 6 nm thick protein bilayer, just as in the case of foam films, which results in strong adhesive interactions between the emulsion drops. The drop-size distribution in hydrophobin stabilized oil-in-water emulsions is investigated at various protein concentrations and oil volume fractions. The data analysis indicates that the emulsification occurs in the Kolmogorov regime or in the regime of limited coalescence, depending on the experimental conditions. The emulsions with HFBII are very stable – no changes in the drop-size distributions are observed after storage for 50 days. However, these emulsions are unstable upon stirring, when they are subjected to the action of shear stresses. This instability can be removed by covering the drops with a second adsorption layer from a conventional protein, like β-lactoglobulin. The HFBII surface layer is able to suppress the Ostwald ripening in the case when the disperse phase is oil that exhibits a pronounced solubility in water. Hence, the hydrophobin can be used to stabilize microcapsules of fragrances, flavors, colors or preservatives due to its dense adsorption layers that block the transfer of oil molecules.