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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
http://psasir.upm.edu.my/id/eprint/113577/
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spelling my.upm.eprints.1135772024-11-13T06:28:33Z http://psasir.upm.edu.my/id/eprint/113577/ Evaluation of bioactive peptides from kenaf (Hibiscus cannabinus L.) seed protein for angiotensin-converting enzyme inhibitory activity 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. 2022-11 Thesis NonPeerReviewed text en http://psasir.upm.edu.my/id/eprint/113577/1/113577.pdf Zaharuddin, Nurul Dhania (2022) Evaluation of bioactive peptides from kenaf (Hibiscus cannabinus L.) seed protein for angiotensin-converting enzyme inhibitory activity. Doctoral thesis, Universiti Putra Malaysia. Kenaf Peptides Angiotensin converting enzyme
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/
language English
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
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
publishDate 2022
url http://psasir.upm.edu.my/id/eprint/113577/1/113577.pdf
http://psasir.upm.edu.my/id/eprint/113577/
_version_ 1816132747427577856
score 13.226497

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