Enhanced O/W emulsifying properties of pea proteins via deamidation: Insights into interfacial behavior.

This study examines the effects of protein glutaminase modification on the interfacial properties and emulsion stability of pea protein isolates (PPI). Emulsions were prepared using native (NPPI) and deamidated PPI (DPPI) at concentrations from 0.5 wt% to 3.6 wt%. The stability of these emulsions was evaluated by examining droplet size distribution, flocculation index, ζ-potential, and CLSM. DPPI demonstrated superior emulsifying ability and stability, requiring only 2.0 wt% to prevent flocculation compared to NPPI's 3.6 wt%. Interfacial properties, such as protein coverage, composition, thickness, tension, and rheology, were characterized. Large Amplitude Oscillatory Dilatation analysis showed minimal differences between NPPI and DPPI-stabilized interfaces at 1 wt%. However, at 3.6 wt%, NPPI interfaces demonstrated abrupt intra-cycle yielding and viscous behavior, whereas DPPI interfaces exhibited gradual softening and a higher maximum linear strain. Additionally, DPPI showed higher interfacial protein coverage and lower interfacial tension. NPPI formed dense, brittle films prone to rupture under dynamic deformation, leading to poor stability. Deamidation of PPI unfolded the protein structure, exposing hydrophobic groups and increasing carboxyl groups, which reduced aggregation. This resulted in a uniform, extensible, and elastic interfacial film resistant to large deformations. Thus, DPPI-stabilized emulsions demonstrated superior stability, showcasing their potential for industrial applications.