<p>This study introduces a novel air frying-assisted deep eutectic solvent (DES) extraction method and investigates its impact on the structural and technofunctional properties of lotus seed protein isolate (LSPI). Compared to the conventional extract (LSPI-Con; 74.08 ± 0.86 mg/g), the air-fried extract (LSPI-AF) exhibited a higher protein yield (122.2 ± 7.3 mg/g) under optimized conditions (protein-to-DES ratio 1:49.2 g/mL, 156.8 ℃, 5.9 min). Structural analyses showed that air frying induced protein modifications. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) revealed high-molecular-weight smears (&gt; 245 kDa), while UV absorbance and increased turbidity indicate reduced solubility and aggregate formation. LSPI-AF also exhibited lower intrinsic fluorescence and a 27% reduction in surface hydrophobicity, suggesting tertiary structure alterations. Fourier transform infrared (FTIR) spectroscopy further revealed shifts in functional group signals, while chemical interaction analysis showed weakened ionic and hydrogen bonds but stronger hydrophobic interactions upon air frying extraction. Despite reduced solubility (69%), LSPI-AF demonstrated improved emulsification behavior, with higher emulsifying activity index (EAI; 330.4 ± 1.2 m²/g) and emulsion stability index (ESI; 1246.0 ± 93.8 min). Emulsion characterization revealed larger droplet sizes (D_4,3 = 260.1 ± 25.0 µm; D_3,2 = 105.2 ± 36.4 µm) but a markedly higher negative zeta potential (− 113.6 ± 3.7 mV), indicating enhanced enhanced electrosatic stabilization. A lower centrifugal precipitation rate (CPR; 3.6 ± 0.3%) and creaming index (CI) further supported the enhanced emulsion-stabilizing capacity of LSPI-AF. Overall, these findings demonstrate that air frying-assisted DES extraction enhances protein recovery and modulates structural characteristics that improve emulsifying performance, which has potential for the development of plant-based emulsifiers.</p>