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Hemp protein hydrolysates with various yields of trichloroacetic acid (TCA)-soluble peptides (Ysp) and surface hydrophobicity (Ho) were obtained by Neutrase® hydrolysis from hemp protein isolate (HPI). The peptide profiles, amino acid composition and antioxidant activities (DPPH radical scavenging ability, reducing power and Fe2+ chelating ability) of the hydrolysates, obtained at 60–240 min, were evaluated. Higher DPPH radical scavenging (IC50, 2.3–2.4 mg/mL) and Fe2+ chelating (IC50, 1.7–1.8 mg/mL) abilities were observed for the hydrolysates with Ysp in the range of 28–30 and 18–28 %, respectively, while the high reducing power was only observed for the hydrolysate with Ysp of 18 %. The DPPH radical scavenging and Fe2+ chelating abilities were closely correlated with the peptide profiles and Ho of the hydrolysates. The peptide profiles of the hydrolysates with higher hydrophobic amino acids exhibited higher DPPH radical scavenging and Fe2+ chelating abilities.