Kinetics of angiotensin -1 converting enzyme inhibition and antioxidative properties of Azadirachta indica seed protein hydrolysates
Neem (Azadirachta indica) seed protein hydrolysates were investigated for in vitro antioxidant and angiotensin 1-converting enzyme (ACE)-inhibitory activities. Neem seed proteins were hydrolysed using pepsin, trypsin and Alcalase. The degree of pepsin hydrolysis of neem seed protein was significantl...
Main Authors: | , , , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
Elsevier
2019-05-01
|
Series: | Heliyon |
Subjects: | |
Online Access: | http://www.sciencedirect.com/science/article/pii/S240584401839176X |
id |
doaj-4abefb4c373a4c17ae6ccdc7def2dd65 |
---|---|
record_format |
Article |
spelling |
doaj-4abefb4c373a4c17ae6ccdc7def2dd652020-11-25T03:46:42ZengElsevierHeliyon2405-84402019-05-0155e01747Kinetics of angiotensin -1 converting enzyme inhibition and antioxidative properties of Azadirachta indica seed protein hydrolysatesRotimi O. Arise0Marvellous A. Acho1Abeeb A. Yekeen2Ibrahim A. Omokanye3Elizabeth O. Sunday-Nwaso4Olatunbosun S. Akiode5Sylvia O. Malomo6Department of Biochemistry, Faculty of Life Sciences, University of Ilorin, P.M.B. 1515, Ilorin, Kwara State, Nigeria; Department of Biological Sciences, College of Science and Engineering, Landmark University, Omu-Aran, Kwara State, Nigeria; Corresponding author.Department of Biochemistry, Faculty of Life Sciences, University of Ilorin, P.M.B. 1515, Ilorin, Kwara State, Nigeria; Department of Biotechnology and Food Technology, Faculty of Applied Sciences, Durban University of Technology, Durban, South AfricaDepartment of Biochemistry, Faculty of Life Sciences, University of Ilorin, P.M.B. 1515, Ilorin, Kwara State, Nigeria; School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, People's Republic of ChinaDepartment of Biochemistry, Faculty of Life Sciences, University of Ilorin, P.M.B. 1515, Ilorin, Kwara State, NigeriaDepartment of Biochemistry, Faculty of Life Sciences, University of Ilorin, P.M.B. 1515, Ilorin, Kwara State, NigeriaSheda Science and Technology Complex, Km 10 from Gwagwalada, Abuja-Lokoja Expressway, Abuja, NigeriaDepartment of Biochemistry, Faculty of Life Sciences, University of Ilorin, P.M.B. 1515, Ilorin, Kwara State, NigeriaNeem (Azadirachta indica) seed protein hydrolysates were investigated for in vitro antioxidant and angiotensin 1-converting enzyme (ACE)-inhibitory activities. Neem seed proteins were hydrolysed using pepsin, trypsin and Alcalase. The degree of pepsin hydrolysis of neem seed protein was significantly higher (p < 0.05) than those of trypsin and Alcalase hydrolysis. Proteolytic hydrolysis of the isolate resulted in hydrolysates with improved Arg/Lys ratio, with pepsin hydrolysates still being able to maintain an acceptable level of essential amino acids comparable to that of the isolate. At 2.5 mg/mL, pepsin neem seed protein hydrolysate (NSPH) demonstrated the strongest antioxidant activity with 67.15 % and 50.07 % DPPH- and superoxide anion radical-scavenging activities, respectively, while trypsin NSPH had the highest ferric-reducing power. Using N-[3-(2-furyl)acryloyl]-L-phenylalanyl-glycyl-glycine (FAPGG) as substrate, NSPHs strongly inhibited ACE (69.20–80.39 %) in a concentration-dependent manner. Pepsin NSPH had higher ACE-inhibitory activity than trypsin and Alcalase NSPHs. Kinetic studies showed the mechanism of ACE inhibition to be mixed-type with Ki values of 0.62, 0.84, 1.5 for pepsin, trypsin and alcalase NSPH, respectively. These results suggest that NSPH can be used as a potential nutraceutical with antioxidant capacity and inhibitory activity against ACE.http://www.sciencedirect.com/science/article/pii/S240584401839176XBiochemistry |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Rotimi O. Arise Marvellous A. Acho Abeeb A. Yekeen Ibrahim A. Omokanye Elizabeth O. Sunday-Nwaso Olatunbosun S. Akiode Sylvia O. Malomo |
spellingShingle |
Rotimi O. Arise Marvellous A. Acho Abeeb A. Yekeen Ibrahim A. Omokanye Elizabeth O. Sunday-Nwaso Olatunbosun S. Akiode Sylvia O. Malomo Kinetics of angiotensin -1 converting enzyme inhibition and antioxidative properties of Azadirachta indica seed protein hydrolysates Heliyon Biochemistry |
author_facet |
Rotimi O. Arise Marvellous A. Acho Abeeb A. Yekeen Ibrahim A. Omokanye Elizabeth O. Sunday-Nwaso Olatunbosun S. Akiode Sylvia O. Malomo |
author_sort |
Rotimi O. Arise |
title |
Kinetics of angiotensin -1 converting enzyme inhibition and antioxidative properties of Azadirachta indica seed protein hydrolysates |
title_short |
Kinetics of angiotensin -1 converting enzyme inhibition and antioxidative properties of Azadirachta indica seed protein hydrolysates |
title_full |
Kinetics of angiotensin -1 converting enzyme inhibition and antioxidative properties of Azadirachta indica seed protein hydrolysates |
title_fullStr |
Kinetics of angiotensin -1 converting enzyme inhibition and antioxidative properties of Azadirachta indica seed protein hydrolysates |
title_full_unstemmed |
Kinetics of angiotensin -1 converting enzyme inhibition and antioxidative properties of Azadirachta indica seed protein hydrolysates |
title_sort |
kinetics of angiotensin -1 converting enzyme inhibition and antioxidative properties of azadirachta indica seed protein hydrolysates |
publisher |
Elsevier |
series |
Heliyon |
issn |
2405-8440 |
publishDate |
2019-05-01 |
description |
Neem (Azadirachta indica) seed protein hydrolysates were investigated for in vitro antioxidant and angiotensin 1-converting enzyme (ACE)-inhibitory activities. Neem seed proteins were hydrolysed using pepsin, trypsin and Alcalase. The degree of pepsin hydrolysis of neem seed protein was significantly higher (p < 0.05) than those of trypsin and Alcalase hydrolysis. Proteolytic hydrolysis of the isolate resulted in hydrolysates with improved Arg/Lys ratio, with pepsin hydrolysates still being able to maintain an acceptable level of essential amino acids comparable to that of the isolate. At 2.5 mg/mL, pepsin neem seed protein hydrolysate (NSPH) demonstrated the strongest antioxidant activity with 67.15 % and 50.07 % DPPH- and superoxide anion radical-scavenging activities, respectively, while trypsin NSPH had the highest ferric-reducing power. Using N-[3-(2-furyl)acryloyl]-L-phenylalanyl-glycyl-glycine (FAPGG) as substrate, NSPHs strongly inhibited ACE (69.20–80.39 %) in a concentration-dependent manner. Pepsin NSPH had higher ACE-inhibitory activity than trypsin and Alcalase NSPHs. Kinetic studies showed the mechanism of ACE inhibition to be mixed-type with Ki values of 0.62, 0.84, 1.5 for pepsin, trypsin and alcalase NSPH, respectively. These results suggest that NSPH can be used as a potential nutraceutical with antioxidant capacity and inhibitory activity against ACE. |
topic |
Biochemistry |
url |
http://www.sciencedirect.com/science/article/pii/S240584401839176X |
work_keys_str_mv |
AT rotimioarise kineticsofangiotensin1convertingenzymeinhibitionandantioxidativepropertiesofazadirachtaindicaseedproteinhydrolysates AT marvellousaacho kineticsofangiotensin1convertingenzymeinhibitionandantioxidativepropertiesofazadirachtaindicaseedproteinhydrolysates AT abeebayekeen kineticsofangiotensin1convertingenzymeinhibitionandantioxidativepropertiesofazadirachtaindicaseedproteinhydrolysates AT ibrahimaomokanye kineticsofangiotensin1convertingenzymeinhibitionandantioxidativepropertiesofazadirachtaindicaseedproteinhydrolysates AT elizabethosundaynwaso kineticsofangiotensin1convertingenzymeinhibitionandantioxidativepropertiesofazadirachtaindicaseedproteinhydrolysates AT olatunbosunsakiode kineticsofangiotensin1convertingenzymeinhibitionandantioxidativepropertiesofazadirachtaindicaseedproteinhydrolysates AT sylviaomalomo kineticsofangiotensin1convertingenzymeinhibitionandantioxidativepropertiesofazadirachtaindicaseedproteinhydrolysates |
_version_ |
1724504837785124864 |