Effect of in vitro gastrointestinal digestion on the Angiotensin Converting Enzyme (ACE) inhibitory activity of pigeon pea protein isolate

Ratnayani K., . and Suter I. K., . and Antara N. S., . and Putra I. N. K., . Effect of in vitro gastrointestinal digestion on the Angiotensin Converting Enzyme (ACE) inhibitory activity of pigeon pea protein isolate. pp. 1397-1404. ISSN 2231-7546

The content of certain bioactive peptides in the gastrointestinal digestive products from legume proteins is expected to provide added value to the function of proteins (beyond the scope of nutrition). In vitro gastrointestinal digestion (GID) involves the hydrolysis of proteins by a mixture of proteases (pepsin trypsin and chymotrypsin) to produce protein hydrolysate. The present work aimed to evaluate the angiotensin converting enzyme (ACE) inhibitory activity of protein hydrolysate produced through a simulated in vitro GID of pigeon pea protein isolates and to fractionate its bioactive peptide component. The protein content of pigeon pea protein isolate was 81.34. The highest value of the degree of hydrolysis and the ACE inhibitory activity was obtained using P‚�‚‚‚TC‚�‚‚‚ treatment (120 min of pepsin followed by 120 min of trypsin-chymotrypsin mixture) with an IC‚‚ value of 64.22 g/mL. The fractionation of the protein hydrolysate using ultra-filtration method resulted in a peptide fraction with the molecular weight below 3 kDa as the most active fraction which had an IC‚‚ value of 11.76 g/ mL and contained 10 peptide components with molecular weight between 400-1 000 Da. These results indicated that the pigeon pea protein hydrolysate has the potential as an ACE inhibitory functional ingredient.

Full text available from: Official URL: http://www.ifrj.upm.edu.my/26%20(04)%202019/30%20-...

Abstract

The content of certain bioactive peptides in the gastrointestinal digestive products from legume proteins is expected to provide added value to the function of proteins (beyond the scope of nutrition). In vitro gastrointestinal digestion (GID) involves the hydrolysis of proteins by a mixture of proteases (pepsin trypsin and chymotrypsin) to produce protein hydrolysate. The present work aimed to evaluate the angiotensin converting enzyme (ACE) inhibitory activity of protein hydrolysate produced through a simulated in vitro GID of pigeon pea protein isolates and to fractionate its bioactive peptide component. The protein content of pigeon pea protein isolate was 81.34. The highest value of the degree of hydrolysis and the ACE inhibitory activity was obtained using P‚�‚‚‚TC‚�‚‚‚ treatment (120 min of pepsin followed by 120 min of trypsin-chymotrypsin mixture) with an IC‚‚ value of 64.22 g/mL. The fractionation of the protein hydrolysate using ultra-filtration method resulted in a peptide fraction with the molecular weight below 3 kDa as the most active fraction which had an IC‚‚ value of 11.76 g/ mL and contained 10 peptide components with molecular weight between 400-1 000 Da. These results indicated that the pigeon pea protein hydrolysate has the potential as an ACE inhibitory functional ingredient.

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Item Type:	Article
AGROVOC Term:	Pigeon peas
AGROVOC Term:	Protein isolates
AGROVOC Term:	In vitro digestibility
AGROVOC Term:	Enzymatic hydrolysis
AGROVOC Term:	Protein hydrolysate
AGROVOC Term:	Inhibition
AGROVOC Term:	Fractionation
AGROVOC Term:	Peptides
AGROVOC Term:	Protein content
AGROVOC Term:	Enzyme inhibitors
Depositing User:	Mr. AFANDI ABDUL MALEK
Last Modified:	24 Apr 2025 00:54
URI:	http://webagris.upm.edu.my/id/eprint/8542

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