pH-driven interfacial selective assembly of gliadin nanoparticles enables high-performance clean-label whipping creams.

Developing clean-label, plant-based whipping creams without low-molecular-weight emulsifiers requires balancing overrun and stability. Herein, we deciphered the pH-dependent multiscale structure-function relationship of gliadin nanoparticle (GNP)-stabilized whipping creams. Emulsions (pH 5.0) prepared near the isoelectric point (pI) achieved superior firmness and ultra-high overrun. To elucidate the stabilization paradox, whereby a significantly increased interfacial protein mass unexpectedly fails to restrict fat coalescence, we decoupled interfacial and continuous-phase interactions. Quantitative proteomics revealed that although pH 5.0 enhanced overall interfacial GNP adsorption, the cross-linking γ-gliadin subfraction was selectively depleted. This structural vulnerability effectively offset the increased protein load, yielding a constant degree of fat partial coalescence. Consequently, macroscopic firmness was fundamentally driven by the continuous phase. Approaching pI induced profound protein unfolding, driving massive intermolecular disulfide cross-linking and hydrophobic interactions that intensified droplet flocculation and serum-phase aggregation. These molecular insights provide a robust physicochemical framework for rationally engineering clean-label aerated food matrices.