The acceptability and marketability of hard-to-cook (HTC) bean has reduced. Protein isolates from HTC bean were hydrolyzed with one of two sequential enzymatic systems: Alcalase-Flavourzyme or pepsin-pancreatin. These hydrolysates were fractionated into five peptide fractions (>10, 5–10, 3–5, 1–3; and <1 kDa) using an ultrafiltration membrane system. Fraction angiotensin I-converting enzyme (ACE) inhibitory (IC50) and antioxidant activities (trolox equivalent antioxidant capacity [TEAC]) were measured: the <1 kDa fractions exhibited the highest values for both activities. These fractions were further purified by gel chromatography in a Sephadex C-50 column (Pharmacia, Uppsala, Sweden), producing 11 peptide fractions (F0-F10) from each <1 kDa fraction. The highest IC50 value (2.7 µg protein/mL) was observed in F6 from the Alcalase-Flavourzyme hydrolysate, and the highest TEAC value (6,922.0 mM/mg sample) was observed in F10 from the pepsin-pancreatin hydrolysate. HTC bean protein hydrolysates and their fractions are promising natural ACE inhibitors and antioxidants, and potential ingredients in functional food systems.