Water lentil (Duckweed), an emerging protein source, is a small floating aquatic plant with agronomic and compositional characteristics rendering it a potential source of bioactive peptides. However, enzymatic hydrolysis of duckweeds has only been carried out to assess the antioxidant and antimicrobial activities of the hydrolysates. The main objectives of this study were to perform enzymatic hydrolysis of duckweed powder utilizing several enzymes and to evaluate the final antihypertensive activity of the fractions. Duckweed powder was efficiently hydrolyzed by pepsin, chymotrypsin, papain and trypsin, with degree of hydrolysis ranging from 3% to 9%, even without prior extraction and concentration of proteins. A total of 485 peptide sequences were identified in the hydrolysates and only 51 were common to two or three hydrolysates. It appeared that phenolic compounds were released through enzymatic hydrolyses and primarily found in the supernatants after centrifugation at concentrations up to 11 mg gallic acid/g sample. The chymotryptic final hydrolysate, the chymotryptic supernatant and the papain supernatant increased the ACE inhibitory activity by more than 6- to 8-folds, resulting in IC50 values ranging between 0.55 to 0.70 mg peptides/mL. Depending on the fraction, the ACE-inhibition was attributed to either bioactive peptides, phenolic compounds or a synergistic effect of both. To the best of our knowledge, this was the first study to investigate the enzymatic hydrolysis of duckweed proteins to produce bioactive peptides with therapeutic applications in mind.
Keywords: ACE-inhibitor; bioactive peptide; duckweed; enzymatic hydrolysis; total phenolic content.