Evaluation of bioactive peptides from kenaf (Hibiscus cannabinus L.) seed protein for angiotensin-converting enzyme inhibitory activity

The aim of this study was to produce bioactive peptides synthesized from kenaf (Hibiscus cannabinus L.) seed, which is a byproduct of the kenaf industry and investigate on its antihypertensive activity. Kenaf seed was observed to produce 12.2 % yield, with 70.2 % protein content. Papain-generated hy...

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Main Author:	Zaharuddin, Nurul Dhania
Format:	Thesis
Language:	English
Published:	2022
Subjects:	Kenaf Peptides Angiotensin converting enzyme
Online Access:	http://psasir.upm.edu.my/id/eprint/113577/1/113577.pdf
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id	my-upm-ir.113577
record_format	uketd_dc
spelling	my-upm-ir.1135772024-11-13T06:28:33Z Evaluation of bioactive peptides from kenaf (Hibiscus cannabinus L.) seed protein for angiotensin-converting enzyme inhibitory activity 2022-11 Zaharuddin, Nurul Dhania The aim of this study was to produce bioactive peptides synthesized from kenaf (Hibiscus cannabinus L.) seed, which is a byproduct of the kenaf industry and investigate on its antihypertensive activity. Kenaf seed was observed to produce 12.2 % yield, with 70.2 % protein content. Papain-generated hydrolysates was observed to produce a very high angiotensin-converting enzyme (ACE) inhibitory activity, with 95.47 %. Therefore, it was decided that papain-generated hydrolysates to be further studied. Optimum condition of 65 °C, pH 6.5, 2.25 hours and E/S ratio 0.03 was determined and produced a maximum degree of hydrolysis (DH) of 58.98 % and 78.45 % ACE inhibitory activity. It was observed that the solubility, foaming and emulsification activity was low at pH 4 and increased up to pH 9 and the water and oil absorption capacity was observed to be lower in kenaf seed protein hydrolysate (KSPH) as compared to kenaf seed protein isolate (KSPI). The in vivo biological activity of KSPH was observed to be the most optimum dosage at 300 mg/kg. Profiling of the peptides showed that peptides with molecular weight 2 to 5 kDa exerted the highest ACE inhibitory (82.27 %) with hydrophobic peptides in the later-eluting fractions. Sequencing showed that peptides INPPSTTN, AKSCVVFP, LLLHAL, WTIPTPS, ALFYWVS and LYWSYLYN possessed high ACE inhibitory activities. Molecular docking reflected that peptide LYWSYLYN with the lowest Glidescore value (-14.66 kJ/mol) possessed the strongest binding affinity towards the ACE protein and kinetic studies discovered that peptide LYWSYLYN which underwent competitive inhibition displayed the lowest Ki value (0.017 mM) which was indicated the most effective ACE inhibitor amongst the other peptides. Thus, it can be concluded that bioactive peptides derived from kenaf seed protein has high ACE inhibitory activity which is a potential functional food ingredient for development of various food applications. Kenaf Peptides Angiotensin converting enzyme 2022-11 Thesis http://psasir.upm.edu.my/id/eprint/113577/ http://psasir.upm.edu.my/id/eprint/113577/1/113577.pdf text en public doctoral Universiti Putra Malaysia Kenaf Peptides Angiotensin converting enzyme Saari, Nazamid
institution	Universiti Putra Malaysia
collection	PSAS Institutional Repository
language	English
advisor	Saari, Nazamid
topic	Kenaf Peptides Angiotensin converting enzyme
spellingShingle	Kenaf Peptides Angiotensin converting enzyme Zaharuddin, Nurul Dhania Evaluation of bioactive peptides from kenaf (Hibiscus cannabinus L.) seed protein for angiotensin-converting enzyme inhibitory activity
description	The aim of this study was to produce bioactive peptides synthesized from kenaf (Hibiscus cannabinus L.) seed, which is a byproduct of the kenaf industry and investigate on its antihypertensive activity. Kenaf seed was observed to produce 12.2 % yield, with 70.2 % protein content. Papain-generated hydrolysates was observed to produce a very high angiotensin-converting enzyme (ACE) inhibitory activity, with 95.47 %. Therefore, it was decided that papain-generated hydrolysates to be further studied. Optimum condition of 65 °C, pH 6.5, 2.25 hours and E/S ratio 0.03 was determined and produced a maximum degree of hydrolysis (DH) of 58.98 % and 78.45 % ACE inhibitory activity. It was observed that the solubility, foaming and emulsification activity was low at pH 4 and increased up to pH 9 and the water and oil absorption capacity was observed to be lower in kenaf seed protein hydrolysate (KSPH) as compared to kenaf seed protein isolate (KSPI). The in vivo biological activity of KSPH was observed to be the most optimum dosage at 300 mg/kg. Profiling of the peptides showed that peptides with molecular weight 2 to 5 kDa exerted the highest ACE inhibitory (82.27 %) with hydrophobic peptides in the later-eluting fractions. Sequencing showed that peptides INPPSTTN, AKSCVVFP, LLLHAL, WTIPTPS, ALFYWVS and LYWSYLYN possessed high ACE inhibitory activities. Molecular docking reflected that peptide LYWSYLYN with the lowest Glidescore value (-14.66 kJ/mol) possessed the strongest binding affinity towards the ACE protein and kinetic studies discovered that peptide LYWSYLYN which underwent competitive inhibition displayed the lowest Ki value (0.017 mM) which was indicated the most effective ACE inhibitor amongst the other peptides. Thus, it can be concluded that bioactive peptides derived from kenaf seed protein has high ACE inhibitory activity which is a potential functional food ingredient for development of various food applications.
format	Thesis
qualification_level	Doctorate
author	Zaharuddin, Nurul Dhania
author_facet	Zaharuddin, Nurul Dhania
author_sort	Zaharuddin, Nurul Dhania
title	Evaluation of bioactive peptides from kenaf (Hibiscus cannabinus L.) seed protein for angiotensin-converting enzyme inhibitory activity
title_short	Evaluation of bioactive peptides from kenaf (Hibiscus cannabinus L.) seed protein for angiotensin-converting enzyme inhibitory activity
title_full	Evaluation of bioactive peptides from kenaf (Hibiscus cannabinus L.) seed protein for angiotensin-converting enzyme inhibitory activity
title_fullStr	Evaluation of bioactive peptides from kenaf (Hibiscus cannabinus L.) seed protein for angiotensin-converting enzyme inhibitory activity
title_full_unstemmed	Evaluation of bioactive peptides from kenaf (Hibiscus cannabinus L.) seed protein for angiotensin-converting enzyme inhibitory activity
title_sort	evaluation of bioactive peptides from kenaf (hibiscus cannabinus l.) seed protein for angiotensin-converting enzyme inhibitory activity
granting_institution	Universiti Putra Malaysia
publishDate	2022
url	http://psasir.upm.edu.my/id/eprint/113577/1/113577.pdf
_version_	1818586155582488576

Evaluation of bioactive peptides from kenaf (Hibiscus cannabinus L.) seed protein for angiotensin-converting enzyme inhibitory activity

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