Abstract

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 ( Y sp), protein composition and surface hydrophobicity ( H o) of the hydrolysates were evaluated. The results showed that the hydrolysates exhibited varying DPPH radical scavenging (with lowest IC 50, ∼2.3 mg/mL) and Fe 2++ chelating (with lowest IC 50 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 Y sp and H o values. The DPPH radical scavenging and Fe 2++ chelating abilities of the hydrolysates were positively correlated with their Y sp or H o values. The results suggest that enzymatic hydrolysis can be used as an effective technique to produce high value-added products of hemp proteins.

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