<p>Legume proteins have attracted growing interest as functional ingredients in food formulations. However, the poor solubility and low emulsifying capacity of legume proteins necessitate physical modifications to improve their functional properties. In this study, mung bean protein (MBP) was subjected to pH-shifting treatment alone (MBP_pH) and in combination with pre-heating and homogenization. The structure, dispersibility, wettability and adsorption behavior of MBP were investigated without and with these pretreatments. The smallest particle size distribution was observed for MBP_pH and its homogenized form, both without and with pre-heating at 65℃. Upon homogenization, the different wettability of the four proteins became comparable, but differences were observed in their adsorption behaviors. The pH-shifting and/or homogenization primarily facilitated protein adsorption onto the oil surface, while pre-heating mainly enhanced interfacial accumulation through protein–protein interactions. After homogenization, all proteins formed a soft viscoelastic layer, but the MBP_pH interfacial layer was more rigid than those of MBP and pre-heated MBP_pH. Camellia seed oil emulsions were characterized in terms of interfacial protein, size distribution, and <InlineEquation ID="IEq1"> <EquationSource Format="TEX">\(\zeta\)</EquationSource> <EquationSource Format="MATHML"><math> <mi>ζ</mi> </math></EquationSource> </InlineEquation>-potential. The most interfacial adsorption was achieved with MBP_pH and 65℃-heated MBP_pH at an oil content of 10% and with pre-heated MBP_pH at an oil content of 30%. However, the emulsified droplets stabilized by MBP and MBP_pH consistently exhibited smaller size distributions than those stabilized by pre-heated MBP_pH. These findings provide valuable insights for the processability of mung bean protein in the food industry.</p>