Generation of bioactive peptides from lentil protein: degree of hydrolysis, antioxidant activity, phenol content, ACE-inhibitory activity, molecular weight, sensory, and functional properties
2021
Rezvankhah, Amir | Yarmand, Mohammad Saeid | Ghanbarzadeh, Babak | Mirzaee, Homaira
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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