Ricinodendron heudelotii kernels were defatted and used as substrate to produce protein hydrolysatesusing papain (PHP), trypsin (PHT), proteases from Abrus precatorius (PHAp)and B. enneandra(PHBe). The degree of hydrolysis (DH), antioxidant (DPPH method), and functional properties of hydrolysates were performed. The DH value, whatever hydrolysis time, was highest with PHP. The water holding capacity decreased with the hydrolysis time from 21.50 ± 0.44% to 5.20 ± 0.07%. After 6h of hydrolysis, PHAp exhibited maximum solubility value (70.17 ± 2.15%) while PHBe had lower solubility value (18.43 ± 0.12%). The highest value of emulsifying activity index was found at pH 9 with 0.25% (w/v) hydrolysate concentration. Within the range of pH used (4-9), the best foam capacity and foam stability were exhibited by PHBe. PHP, PHAp, and PHT inhibited DPPH radical at 83.30 ± 0.46, 75.07 ± 0.15, and 56.78 ± 0.40%, respectively, at 6h of hydrolysis.