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This study aimed to hydrolyze lentil protein from two hydrolysis stages: single and sequential hydrolysis using Alcalase (1, 2, and 4% w/w enzyme to substrate (E:S)) and Flavourzyme (2% w/w) through a processing time of 180 min with an interval of 30 min, and then, degree of hydrolysis (DH), antioxidant and angiotensin-converting enzyme (ACE)-inhibitory activities, phenolic compounds, amino acid composition, molecular weight (MW) distribution, molecular weight profile, sensory, and functional properties were evaluated. The highest DH (47.05%), ACE-inhibitory (0.25 mg/mL), and phenolic compounds (3.84 mg GAE/g) were obtained when sequential hydrolysis was accomplished at Alcalase and Flavourzyme concentrations of 2% w/w and hydrolysis time of 120 and 60 min, respectively. Hydrolysis did not change the main amino acid profile. Despite this, the amino acids which contribute to umami taste were increased after hydrolysis. According to Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) results, the lowest MW peptides were produced by sequential hydrolysis which was agreed by gel permeation chromatography (GPC) (4.4 kDa and 100 Da). Sensorial analysis indicated that peptides produced by Alcalase at 1% w/w concentration with hydrolysis time of 180 min (Al-1%-180 min, DH value of 15.72%) had the highest bitter taste and further hydrolysis led to reduction of bitter taste and sweetness was increased for Flavourzyme (Fl-2%-180 min) and also sequential hydrolysis produced peptides. Alcalase digests indicated higher solubility than control and Flavourzyme digest. The emulsifying activity index (EAI) was decreased (35.2 to 21.5%) while Foaming capacity (FC) was increased (80 to 104.76%) by Alcalase hydrolysis.

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This study aimed to produce bioactive peptides with increased angiotensin‐converting enzyme (ACE)‐inhibitory and antioxidant activities from single and sequential hydrolysis, using Alcalase and Flavourzyme at the enzyme to substrate ratio of 2% and hydrolysis time of 180 min. Results indicated that sequential hydrolysis led to a higher degree of hydrolysis (DH) value (47.05%) compared with single hydrolysis (8.51% and 20.12%). Higher ACE‐inhibitory activity and total phenol content were determined for the lentil protein hydrolysates (LPH) compared with lentil protein concentrate, and also higher antioxidant activity was obtained comparing with butylated hydroxytoluene as a synthetic antioxidant. The main amino acid profile of hydrolysates was maintained. The higher DH via hydrolysis was obtained, more small and medium molecular weight peptides were generated according to the gel permeation chromatography and sodium dodecyl sulfate–polyacrylamide gel electrophoresis. Hydrolysis did not have a significant effect on the denaturation point of protein, and thus the thermal stability was maintained. Shorter peaks were observed for hydrolysates by atomic force microscopy. Enzymatic hydrolysis increased the umami sensorial taste. Novelty impact statement Using a combination of enzymes in sequential hydrolysis can produce bioactive peptides with improved ACE‐inhibitory and antioxidant activities. Alcalase leads to the production of bitter taste peptides which can be altered by applying Flavourzyme to hydrolyze the former peptides to fewer bitter peptides. Lentil protein was hydrolyzed sequentially into bioactive peptides with improved anti‐hypertensive and antioxidant activities and increment of umami taste in respect to the produced peptides with specific amino acid profiles.