Adhesion behaviors of egg white proteins to stainless steel (SS) surfaces at pH 7.4 and 30°C are reported. Ovalbumin and ovomucoid, acidic egg white proteins, were less adsorbed in the presence of phosphate (Pi), a multivalent anion, than in the presence of HEPES, an amphoteric ion. In contrast, lysozyme, a basic egg white protein, was more adsorbed in the presence of Pi than in the presence of HEPES. Citrate, another multivalent anion, and taurin, another amphoteric ion, affected the adsorption of these egg white proteins in a manner similar to Pi and HEPES, respectively. Based on the knowledge thus far obtained on the adhesion mode of several proteins to SS surfaces, these observations can be explained by assuming that small ionic substances precede proteins in attaching to SS surfaces, resulting in the alteration of effective surface charge. These findings could lead to the development of strategies for suppression of acidic egg white protein adhesion.