Ovalbumin and ovotransferrin are two proteins in hen egg white with isoelectric points of 4.8 and 6.8, respectively. A convenient and green method was developed in this study to prepare ovalbumin-ovotransferrin nanogels: a mixture of the two proteins was adjusted to a certain pH and then heated. Heat induced denaturation and gelation of the proteins, but the negative charges of ovalbumin prevented the proteins from coagulating. Dynamic light scattering, transmission electron microscopy, and atomic force microscopy studies reveal the nanogels have a spherical shape in both the swell and dry forms. Their apparent hydrodynamic diameters are in the range of 100-220 nm depending on the protein concentration in the nanogel preparation process. The nanogels display an amphoteric property: they carry net positive charges at pH lower than 5.5 and net negative charges at pH higher than 5.5. They form redispersible secondary aggregates at pH 5.0-6.0. The nanogels are stable in the pH ranges of 2.0-4.0 and 7.0-11.0, and they exhibit pH unchangeable but thermoreversible hydrophobicity. Benzoic acid was used as a model drug to study the loading ability. The native ovalbumin and ovotransferrin cannot bind with benzoic acid, whereas the nanogels with the network structure and hydrophobic binding sites can load benzoic acid through hydrophobic and electrostatic interactions.