To　overcome　hydrophobicity　and　chemical　instability　of　resveratrol　(Rev),　modified　whey　protein　isolate　(WPI)　and　gelatin　(Gel)　were　used　to　load　Rev.　Three　treatments　including　pH-shifting　at　pH　12　(S),　pH-shifting　at　pH　12　combined　with　ultrasonication　at　pH　7　(SU7),　and　pH-shifting　at　pH　12　combined　with　ultrasonication　at　pH　12　(SU12)　were　conducted　to　obtain　a　series　of　modified　proteins　(WPI-S,　WPI-SU7,　WPI-SU12,　Gel-S,　Gel-SU7,　Gel-SU12).　Among　them,　WPI-SU12　and　Gel-SU12　had　the　highest　encapsulation　efficiency　(EE)　and　loading　capacity　(LC)　for　Rev.　The　EE　and　LC　were　92.69　?　0.25%　and　17.37　?　0.067　g/100　g　protein　in　WPI-SU12-Rev　nanocomposite,　respectively,　and　83.85　?　0.43%　and　15.68　?　0.070　g/100　g　protein　in　Gel-SU12-Rev　nanocomposite,　respectively.　This　might　be　related　to　the　highest　surface　hydrophobicity　of　modified　proteins　in　SU12　groups.　The　particle　sizes　of　all　nanocomposites　were　below　200　nm,　while　the　higher　?-potential　absolute　value　of　WPI-SU12-Rev　nanocomposite　than　that　of　Gel-SU12-Rev　nanocomposite　indicated　higher　stability.　Molecular　interaction　and　secondary　structure　analysis　verified　that　the　proteins　and　Rev　bound　to　each　other.　Moreover,　protein　nanocomposites　could　greatly　improve　the　water　solubility　and　antioxidant　capacity　of　Rev.　In　summary,　the　WPI　modified　by　ultrasonication　at　pH　12　showed　the　best　loading　with　Rev.