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Identification, molecular docking, and kinetic studies of six novel angiotensin-I-converting enzyme (ACE) inhibitory peptides derived from Kenaf (Hibiscus cannabinus L.) seed

Kenaf (Hibiscus cannabinus L.) seed is a valuable protein source that could be used to prepare protein hydrolysates with antihypertensive properties. However, the potential of using kenaf seeds for health food and pharmaceutical applications has not been fully exploited. Thus, the aim of this study...

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Main Authors: Zaharuddin, Nurul Dhania, Barkia, Ines, Wan Ibadullah, Wan Zunairah, Zarei, Mohammad, Saari, Nazamid
Format: Article
Published: Elsevier 2022
Online Access:http://psasir.upm.edu.my/id/eprint/101767/
https://www.sciencedirect.com/science/article/pii/S0141813022020736
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spelling my.upm.eprints.1017672023-10-16T02:51:16Z http://psasir.upm.edu.my/id/eprint/101767/ Identification, molecular docking, and kinetic studies of six novel angiotensin-I-converting enzyme (ACE) inhibitory peptides derived from Kenaf (Hibiscus cannabinus L.) seed Zaharuddin, Nurul Dhania Barkia, Ines Wan Ibadullah, Wan Zunairah Zarei, Mohammad Saari, Nazamid Kenaf (Hibiscus cannabinus L.) seed is a valuable protein source that could be used to prepare protein hydrolysates with antihypertensive properties. However, the potential of using kenaf seeds for health food and pharmaceutical applications has not been fully exploited. Thus, the aim of this study was to identify and characterise the Angiotensin-I-Converting Enzyme (ACE) inhibitory peptides derived from the optimized hydrolysis conditions of kenaf seed protein hydrolysates (KSPH). The optimum hydrolysis conditions determined by response surface methodology (RSM) were as follows: temperature 65 °C, pH 6.5, hydrolysis time 2.25 h, and enzyme/substrate (E/S) ratio of 0.03 (w/w). Under these conditions, the degree of hydrolysis (DH) was 55.28 % and ACE inhibitory activity was 75.51 %. Also, the low molecular weight peptide fractions, <2 kilodalton (kDa) and 2–5 kDa showed the highest ACE-inhibitory activity (82.27 % and 83.69 %, respectively). The 2–5 kDa fraction by Quadrupole-Time-of-Flight Liquid Chromatography-Mass Spectrometry (QTOF LC − MS) revealed the abundance of six peptides, LYWSYLYN, ALFYWVS, LLLHAL, AKSCVVFP, INPPSTTN, and WTIPTPS. Kinetic studies showed that peptide LYWSYLYN possessed the highest Michaelis constant (Km), maximum velocity (Vmax) values and the lowest inhibitor constant (Ki) values, suggesting of its superior ACE inhibitory activity compared to other peptides. Elsevier 2022 Article PeerReviewed Zaharuddin, Nurul Dhania and Barkia, Ines and Wan Ibadullah, Wan Zunairah and Zarei, Mohammad and Saari, Nazamid (2022) Identification, molecular docking, and kinetic studies of six novel angiotensin-I-converting enzyme (ACE) inhibitory peptides derived from Kenaf (Hibiscus cannabinus L.) seed. International Journal of Biological Macromolecules, 220. 1512 - 1522. ISSN 0141-8130; ESSN: 1879-0003 https://www.sciencedirect.com/science/article/pii/S0141813022020736 10.1016/j.ijbiomac.2022.09.142
institution Universiti Putra Malaysia
building UPM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Putra Malaysia
content_source UPM Institutional Repository
url_provider http://psasir.upm.edu.my/
description Kenaf (Hibiscus cannabinus L.) seed is a valuable protein source that could be used to prepare protein hydrolysates with antihypertensive properties. However, the potential of using kenaf seeds for health food and pharmaceutical applications has not been fully exploited. Thus, the aim of this study was to identify and characterise the Angiotensin-I-Converting Enzyme (ACE) inhibitory peptides derived from the optimized hydrolysis conditions of kenaf seed protein hydrolysates (KSPH). The optimum hydrolysis conditions determined by response surface methodology (RSM) were as follows: temperature 65 °C, pH 6.5, hydrolysis time 2.25 h, and enzyme/substrate (E/S) ratio of 0.03 (w/w). Under these conditions, the degree of hydrolysis (DH) was 55.28 % and ACE inhibitory activity was 75.51 %. Also, the low molecular weight peptide fractions, <2 kilodalton (kDa) and 2–5 kDa showed the highest ACE-inhibitory activity (82.27 % and 83.69 %, respectively). The 2–5 kDa fraction by Quadrupole-Time-of-Flight Liquid Chromatography-Mass Spectrometry (QTOF LC − MS) revealed the abundance of six peptides, LYWSYLYN, ALFYWVS, LLLHAL, AKSCVVFP, INPPSTTN, and WTIPTPS. Kinetic studies showed that peptide LYWSYLYN possessed the highest Michaelis constant (Km), maximum velocity (Vmax) values and the lowest inhibitor constant (Ki) values, suggesting of its superior ACE inhibitory activity compared to other peptides.
format Article
author Zaharuddin, Nurul Dhania
Barkia, Ines
Wan Ibadullah, Wan Zunairah
Zarei, Mohammad
Saari, Nazamid
spellingShingle Zaharuddin, Nurul Dhania
Barkia, Ines
Wan Ibadullah, Wan Zunairah
Zarei, Mohammad
Saari, Nazamid
Identification, molecular docking, and kinetic studies of six novel angiotensin-I-converting enzyme (ACE) inhibitory peptides derived from Kenaf (Hibiscus cannabinus L.) seed
author_facet Zaharuddin, Nurul Dhania
Barkia, Ines
Wan Ibadullah, Wan Zunairah
Zarei, Mohammad
Saari, Nazamid
author_sort Zaharuddin, Nurul Dhania
title Identification, molecular docking, and kinetic studies of six novel angiotensin-I-converting enzyme (ACE) inhibitory peptides derived from Kenaf (Hibiscus cannabinus L.) seed
title_short Identification, molecular docking, and kinetic studies of six novel angiotensin-I-converting enzyme (ACE) inhibitory peptides derived from Kenaf (Hibiscus cannabinus L.) seed
title_full Identification, molecular docking, and kinetic studies of six novel angiotensin-I-converting enzyme (ACE) inhibitory peptides derived from Kenaf (Hibiscus cannabinus L.) seed
title_fullStr Identification, molecular docking, and kinetic studies of six novel angiotensin-I-converting enzyme (ACE) inhibitory peptides derived from Kenaf (Hibiscus cannabinus L.) seed
title_full_unstemmed Identification, molecular docking, and kinetic studies of six novel angiotensin-I-converting enzyme (ACE) inhibitory peptides derived from Kenaf (Hibiscus cannabinus L.) seed
title_sort identification, molecular docking, and kinetic studies of six novel angiotensin-i-converting enzyme (ace) inhibitory peptides derived from kenaf (hibiscus cannabinus l.) seed
publisher Elsevier
publishDate 2022
url http://psasir.upm.edu.my/id/eprint/101767/
https://www.sciencedirect.com/science/article/pii/S0141813022020736
_version_ 1781706705337319424
score 13.211869

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