This study investigated the effect of interfacial rigidity on the tunable rheol. properties of high internal phase Pickering emulsions (HIPPEs).To produce protein samples with varying degrees of flexibility, walnut protein isolate (WPI) was complexed with casein (CA) through a pH shifting method and further crosslinked with genipin.CA/WPI and genipin-crosslinked CA/WPI (G-CA/WPI) nanocomplexes exhibited significantly decreased particle sizes (lower than 150 nm), increased β-sheet content, and enhanced rigidity.While CA/WPI and G-CA/WPI demonstrated appropriate wettability (close to 90°), their interfacial tensions were relatively higher than that of CA by 2.5-5 mN/m.Notably, the quartz crystal microbalance (QCM) study revealed that the oil-water interface adsorbed with CA/WPI and G-CA/WPI exhibited significantly greater interfacial rigidity (low dissipation shifts <1.2 x 10-6) than those adsorbed with CA, WPI, or their mixture (M-CA/WPI).The HIPPEs stabilized by 2% CA/WPI and G-CA/WPI exhibited comparable oil droplet sizes to those stabilized by CA or M-CA/WPI, yet they demonstrated significantly enhanced storage modulus by 1.5-5-fold and increased critical stresses by up to 25-fold, indicating their improved viscoelastic properties.Lissajous-Bowditch curves further confirmed that the HIPPEs fabricated with CA/WPI and G-CA/WPI were more resistant to deformation.These findings underscore the pivotal role of protein particle rigidity in the rheol. properties of stabilized HIPPEs, guiding the design of novel HIPPEs with tailored applications.