High angiotensin-I converting enzyme (ACE) inhibitory activity of Alcalase-digested green soybean (Glycine max) hydrolysates

• Published in: Food research international 2018-04, Vol.106, p.589-597
• Main Authors: Hanafi, Mohamad Ariff, Hashim, Siti Nadia, Chay, Shyan Yea, Ebrahimpour, Afshin, Zarei, Mohammad, Muhammad, Kharidah, Abdul-Hamid, Azizah, Saari, Nazamid
• Format: Article
• Language: English
• Subjects: ACE inhibitory activity; Angiotensin-Converting Enzyme Inhibitors - isolation & purification; Angiotensin-Converting Enzyme Inhibitors - pharmacology; Antihypertensive Agents - isolation & purification; Antihypertensive Agents - pharmacology; Bioactive peptides; Bromelains - chemistry; Endopeptidases - chemistry; Food Handling - methods; Functional food; Glycine max - chemistry; Green soybean; Hydrolysate; Hydrolysis; Papain - chemistry; Peptides - isolation & purification; Peptides - pharmacology; Protein Hydrolysates - isolation & purification; Protein Hydrolysates - pharmacology; Proteolysis; Soybean Proteins - isolation & purification; Soybean Proteins - pharmacology; Subtilisins - chemistry; Time Factors
• ISSN: 0963-9969; 1873-7145
• DOI: 10.1016/j.foodres.2018.01.030

As a protein-rich, underutilized crop, green soybean could be exploited to produce hydrolysates containing angiotensin-I converting enzyme (ACE) inhibitory peptides. Defatted green soybean was hydrolyzed using four different food-grade proteases (Alcalase, Papain, Flavourzyme and Bromelain) and their ACE inhibitory activities were evaluated. The Alcalase-generated green soybean hydrolysate showed the highest ACE inhibitory activity (IC50: 0.14 mg/mL at 6 h hydrolysis time) followed by Papain (IC50: 0.20 mg/mL at 5 h hydrolysis time), Bromelain (IC50: 0.36 mg/mL at 6 h hydrolysis time) and Flavourzyme (IC50: 1.14 mg/mL at 6 h hydrolysis time) hydrolysates. The Alcalase-generated hydrolysate was profiled based on its hydrophobicity and isoelectric point using reversed phase high performance liquid chromatography (RP-HPLC) and isoelectric point focusing (IEF) fractionators. The Alcalase-generated green soybean hydrolysate comprising of peptides EAQRLLF, PSLRSYLAE, PDRSIHGRQLAE, FITAFR and RGQVLS, revealed the highest ACE inhibitory activity of 94.19%, 99.31%, 92.92%, 101.51% and 90.40%, respectively, while their IC50 values were 878 μM, 532 μM, 1552 μM, 1342 μM and 993 μM, respectively. It can be concluded that Alcalase-digested green soybean hydrolysates could be exploited as a source of peptides to be incorporated into functional foods with antihypertensive activity. [Display omitted] •Proteolysis of green soybean (Glycine max) proteins yields hydrolysates with ACE inhibitory activity.•IC50 of Alcalase-generated green soybean hydrolysate after 6 h was 0.14 mg/mL.•Hydrophobic and hydrophilic peptides contribute equally towards high ACE inhibitory activity.•Five of the peptides revealed high ACE inhibitory activity.