ACE-inhibitory activity of seed storage proteins and hydrolysates from Job’s tears (Coix lacryma-jobi L.)

Sarnthima, R. and Khammuang, S. and Sanachai, K. (2023) ACE-inhibitory activity of seed storage proteins and hydrolysates from Job’s tears (Coix lacryma-jobi L.). International Food Research Journal (Malaysia), 30. pp. 439-446. ISSN 2231 7546

Though hypertension is a serious health problem, the inhibition of the angiotensin-I converting enzyme (ACE) provides a means to treat and manage it. In the present work, we investigated the ACE-inhibitory activity of crude proteins and protein hydrolysates from Job’s tears (Coix lacryma-jobi L.). ACE inhibition of 22.15 ± 0.94% was observed with 400 µg of protein from Job’s tears as compared to captopril, a common ACE inhibitor, equaled to 53.7 ± 2.3 nmol captopril equivalent per mg of protein (IC50 of captopril towards ACE was 4.8 nmol). The crude proteins from Job’s tears were enzymatically hydrolysed for 1, 2, and 3 h (E/S of 1:20 by weight) using commercial proteolytic enzymes including Alcalase, Papain, Pronase, and Trypsin. All hydrolysates exhibited increased ACE-inhibitory activity. The protein hydrolysates (400 µg) prepared using Pronase for 2 h (CLPrH-2h) exhibited the highest inhibitory activity (78.38 ± 0.23% or 190.0 ± 0.5 nmol captopril equiv. per mg protein) and were ~3.5 times more active as compared to the crude proteins. Fractionation of the peptides was performed using semi-preparative reversephase high-performance liquid chromatography (RP-HPLC), and all the fractions exhibited ACE-inhibitory activity. The most active fraction was F2 (41.58% inhibition) which was ~7.5 times more active than the crude proteins. These results suggested that seeds from Job’s tears could be an interesting source for developing functional foods with antihypertensive properties.

Full text available from: Official URL: http://www.ifrj.upm.edu.my/30%20(02)%202023/14%20-...

Abstract

Though hypertension is a serious health problem, the inhibition of the angiotensin-I converting enzyme (ACE) provides a means to treat and manage it. In the present work, we investigated the ACE-inhibitory activity of crude proteins and protein hydrolysates from Job’s tears (Coix lacryma-jobi L.). ACE inhibition of 22.15 ± 0.94% was observed with 400 µg of protein from Job’s tears as compared to captopril, a common ACE inhibitor, equaled to 53.7 ± 2.3 nmol captopril equivalent per mg of protein (IC50 of captopril towards ACE was 4.8 nmol). The crude proteins from Job’s tears were enzymatically hydrolysed for 1, 2, and 3 h (E/S of 1:20 by weight) using commercial proteolytic enzymes including Alcalase, Papain, Pronase, and Trypsin. All hydrolysates exhibited increased ACE-inhibitory activity. The protein hydrolysates (400 µg) prepared using Pronase for 2 h (CLPrH-2h) exhibited the highest inhibitory activity (78.38 ± 0.23% or 190.0 ± 0.5 nmol captopril equiv. per mg protein) and were ~3.5 times more active as compared to the crude proteins. Fractionation of the peptides was performed using semi-preparative reversephase high-performance liquid chromatography (RP-HPLC), and all the fractions exhibited ACE-inhibitory activity. The most active fraction was F2 (41.58% inhibition) which was ~7.5 times more active than the crude proteins. These results suggested that seeds from Job’s tears could be an interesting source for developing functional foods with antihypertensive properties.

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Item Type:	Article
AGROVOC Term:	Coix lacryma-jobi
AGROVOC Term:	protein hydrolysates
AGROVOC Term:	hydrolysis
AGROVOC Term:	enzyme activity
AGROVOC Term:	bioactive compounds
AGROVOC Term:	functional foods
Geographical Term:	Thailand
Depositing User:	Nor Hasnita Abdul Samat
Date Deposited:	30 Jun 2025 08:37
Last Modified:	30 Jun 2025 08:37
URI:	http://webagris.upm.edu.my/id/eprint/557

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