Chicken ovalbumin (OVA) and lysozyme (LZ) are important biological products, which come from the egg‐white. However, the separation of OVA and LZ is realized by traditional salting‐out method needing large amount of ammonium sulfate, leading to lysozyme enzyme activity reducing. In this work, we used a tropine‐based ionic liquid (IL) hydrogel to separate OVA and LZ. The adsorption isotherms, thermodynamics and kinetics were investigated. The IL gel showed maximum adsorption capacity of 926 mg g−1 for OVA, nearly 152 % higher than that reported in other literature. Moreover, the secondary structure of desorbed OVA was confirmed by fluorescence spectroscopy (FL), circular dichroism spectra (CD) and differential scanning calorimetry (DSC). The material presented high OVA adsorption capacity, excellent OVA selectivity and good biocompatibility in OVA‐LZ protein system. It could be considered as a promising material for preferential protein adsorption, at least for separation of OVA and LZ.