Curcumin＇s　(Cur,　C)　utility　is　restricted　by　poor　solubility,　stability,　and　bioavailability.　This　study　optimized　zein　(Z)-centered　core-shell　nanoparticles　using　soluble　pea　protein　(Psup)　or　whey　protein　isolate　(WPI,　W)　as　the　shell.　pH-shifting　enhanced　Cur　loading　to　316.3　μg/mg　(PsupZC)　and　266.1　μg/mg　(WZC),　surpassing　simple　complexation,　which　left　exposed　Cur　crystals　after　lyophilization.　Core-shell　ratios　controls　particle　sizes　(50–102　nm　for　PsupZC;　30–80　nm　for　WZC)　with　polydispersity　index＜0.2.　PsupZC　demonstrated　enhanced　photostability,　thermal　stability,　and　retained　over　65　%　Cur　under　gastric　conditions,　outperforming　WZC.　Mechanistically,　the　proteins＇　hydrophobicity　facilitated　stronger　interactions　with　Cur,　while　pH-shifting　enhanced　cur-protein　binding　through　hydrogen　bonding.　Cur　incorporation　stabilized　protein　secondary　structures,　increasing　α-helix　and　β-sheet　content.　Furthermore,　these　nanoparticles　were　also　able　to　stabilize　Pickering　emulsions.　Overall,　pH-shifting,　core-shell　compositions　and　optimized　ratios　enabled　tailored　PsupZ　nanoparticles,　providing　more　scalable　and　multifunctional　protein-based　carriers　for　hydrophobic　bioactives.　©　2024