Abstract
Peptide with hydrophobic amino acids had been studied for their inhibitory activity against angiotensin-I converting enzyme (ACE-1) transformation into ACE-2 and prevention of hypertension. The active peptides may come from alcalase and flavourzyme hydrolysis of bean protein. This study aimed to measure ACE-1 inhibitory of protein hydrolysates from Vigna sp. bean (mung bean and cowpea) that grew in Indonesia, and its solubility. The bean protein (22.9 - 23.6 %) was extracted using isoelectric precipitation at pH 4-4.6. The extracts were hydrolyzed at pH 8 for alcalase and pH 7 for flavourzyme, followed with inactivation at 80-85 oC. ACE-1 inhibitory activity was calculated based on the amount of hippuric acid (HA) formed by the hydrolysis of Hippuryl-His-Leu (HHL), in spectrophotometry detection method (228 nm). Ultrachromatography evaluation showed that the protein hydrolysates of mungbean contained higher hydrophobic amino acids (382 mg/g protein) compared to those of cowpea (329 mg/g protein). Protein hydrolysates of both beans from alcalase hydrolysis have higher ACE-1 inhibitory activity rather than those from flavourzyme. Protein hydrolysate from Vigna spp bean protein hydrolysis by alcalase, contained small molecular weight peptides (3.9-4.63 kDa) and high ACE-1 inhibition ability (80-93 %), and therefore suggested as antihypertensive nutraceuticals. Highest solubility of protein hydrolysates resulted from alcalase hydrolysis of both beans were observed at pH 8, while those resulted from flavorzyme hydrolysis were at pH 7, respectively.
Highlights
The alcalase and flavourzyme hydrolysed protein of mungbean and cowpea grown in Indonesia, were 2020:2(1), pp
Able to inhibit the activity of angiotensin-I converting enzyme (ACE-I) with inhibitory values greater than 70 percent
The amount of hydrophobic amino acids in mungbean protein extract that hydrolysed by alcalase, was higher than that of in cowpea protein extract
Summary
The bean protein hydrolysate was able to inhibit the ACE-I action in becoming ACE-2, that stimulated aldosterone secretion and increased blood pressure. Such beans were grown in Indonesia, and though not yet studied before, protein hydrolysates coming from Indonesian beans may be a potential source of natural functional ingredients or nutraceuticals with ACE1 inhibitor or antihypertensive activities. The angiotensin-1 converting enzyme (ACE-1) inhibitory ability arises from the action of protein hydrolysates that containing a mixture of shortchain peptides (2-15 amino acid residues) with hydrophobic amino acids at their end sites, such as Arg-Lys, Val-Ala-Pro, Phe-Val-Ala-Pro, and TryPhe-Trp-Leu. Previous studies shown that the peptide composition in bean protein hydrolysates consist of hydrophobic amino acids at the end side of its chain, that are leusine (Leu), phenylalanine (Phe), valine (Val) and isoleucine (Ileu). Various studies have shown that bean protein hydrolysates antihypertensive activity were correlated to their performance in inhibiting ACE-1 activity (Arihara et al, 2000; Daskaya-Dikem et al, 2017; Nakamura et al, 1995; Torruco-Uco et al, 2009)
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
