Enzymatic hydrolysis of hemp (Cannabis sativa L.) protein isolate by various proteases and antioxidant properties of the resulting hydrolysates

Enzymatic hydrolysis of hemp protein isolate (HPI) by six proteases (alcalase, flavourzyme, neutrase, protamex, pepsin and trypsin) and antioxidant activities of the resulting hydrolysates, obtained for 2 and 4 h were investigated. The yield of trichloroacetic acid (TCA)-soluble peptides (Ysp), protein composition and surface hydrophobicity (Ho) of the hydrolysates were evaluated. The results showed that the hydrolysates exhibited varying DPPH radical scavenging (with lowest IC50, ∼2.3 mg/mL) and Fe2++ chelating (with lowest IC50 of 1.6–1.7 mg/mL) abilities and reducing power (with highest absorbance at 700 nm of 0.31–0.35), depending on their Ysp and Ho values. The DPPH radical scavenging and Fe2++ chelating abilities of the hydrolysates were positively correlated with their Ysp or Ho values. The results suggest that enzymatic hydrolysis can be used as an effective technique to produce high value-added products of hemp proteins.