Kinetics of the inhibition of renin and angiotensin I-converting enzyme by cod (Gadus morhua) protein hydrolysates and their antihypertensive effects in spontaneously hypertensive rats
Background: Cod muscle has a balanced protein profile that contains potentially bioactive amino acid sequences. However, there is limited information on release of these peptides from the parent proteins and their ability to modulate mammalian blood pressure. Objective: The aim of this study was to...
Published in: | Food & Nutrition Research |
---|---|
Main Authors: | , , , , , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
Swedish Nutrition Foundation
2015
|
Subjects: | |
Online Access: | https://doi.org/10.3402/fnr.v59.29788 https://doaj.org/article/bd5990fd04e5469297a8ae0506f98631 |
id |
ftdoajarticles:oai:doaj.org/article:bd5990fd04e5469297a8ae0506f98631 |
---|---|
record_format |
openpolar |
spelling |
ftdoajarticles:oai:doaj.org/article:bd5990fd04e5469297a8ae0506f98631 2023-05-15T16:19:24+02:00 Kinetics of the inhibition of renin and angiotensin I-converting enzyme by cod (Gadus morhua) protein hydrolysates and their antihypertensive effects in spontaneously hypertensive rats Abraham T. Girgih Ifeanyi D. Nwachukwu Fida Hasan Tayo N. Fagbemi Tom Gill Rotimi E. Aluko 2015-12-01T00:00:00Z https://doi.org/10.3402/fnr.v59.29788 https://doaj.org/article/bd5990fd04e5469297a8ae0506f98631 EN eng Swedish Nutrition Foundation http://www.foodandnutritionresearch.net/index.php/fnr/article/view/29788/44348 https://doaj.org/toc/1654-661X 1654-661X doi:10.3402/fnr.v59.29788 https://doaj.org/article/bd5990fd04e5469297a8ae0506f98631 Food & Nutrition Research, Vol 59, Iss 0, Pp 1-9 (2015) cod protein hydrolysate angiotensin I-converting enzyme renin enzyme inhibition kinetics IC50 systolic blood pressure spontaneously hypertensive rats Nutrition. Foods and food supply TX341-641 article 2015 ftdoajarticles https://doi.org/10.3402/fnr.v59.29788 2022-12-30T21:51:31Z Background: Cod muscle has a balanced protein profile that contains potentially bioactive amino acid sequences. However, there is limited information on release of these peptides from the parent proteins and their ability to modulate mammalian blood pressure. Objective: The aim of this study was to generate cod antihypertensive peptides with potent in vitro inhibitory effects against angiotensin-converting enzyme (ACE) and renin. The most active peptides were then tested for systolic blood pressure (SBP)-reducing ability in spontaneously hypertensive rats (SHRs). Design: Cod protein hydrolysate (CPH) was produced by subjecting the muscle proteins to proteolysis first by pepsin and followed by trypsin+chymotrypsin combination. In order to enhance peptide activity, the CPH was subjected to reverse-phase (RP)-HPLC separation to yield four fractions (CF1, CF2, CF3, and CF4). The CPH and RP-HPLC fractions were each tested at 1 mg/mL for ability to inhibit in vitro ACE and renin activities. CPH and the most active RP-HPLC fraction (CF3) were then used for enzyme inhibition kinetics assays followed by oral administration (200 and 30 mg/kg body weight for CPH and CF3, respectively) to SHRs and SBP measurements within 24 h. Results: The CPH, CF3, and CF4 had similar ACE-inhibitory activities of 84, 85, and 87%, which were significantly (p<0.05) higher than the values for CF1 (69%) and CF2 (79%). Conversely, the CF3 had the highest (63%) renin-inhibitory activity (p<0.05) when compared to CPH (43%), CF1 (15%), and CF4 (44%). CPH and CF3 exhibited uncompetitive mode of ACE inhibition, whereas renin inhibition was non-competitive. Even at a 6.7-fold lower dosage, the CF3 significantly (p<0.05) reduced SBP (maximum −40.0 mmHg) better than CPH (maximum −19.1 mmHg). Conclusions: RP-HPLC fractionation led to enhanced antihypertensive effects of cod peptides, which may be due to a stronger renin-inhibitory activity. Article in Journal/Newspaper Gadus morhua Directory of Open Access Journals: DOAJ Articles Food & Nutrition Research 59 1 29788 |
institution |
Open Polar |
collection |
Directory of Open Access Journals: DOAJ Articles |
op_collection_id |
ftdoajarticles |
language |
English |
topic |
cod protein hydrolysate angiotensin I-converting enzyme renin enzyme inhibition kinetics IC50 systolic blood pressure spontaneously hypertensive rats Nutrition. Foods and food supply TX341-641 |
spellingShingle |
cod protein hydrolysate angiotensin I-converting enzyme renin enzyme inhibition kinetics IC50 systolic blood pressure spontaneously hypertensive rats Nutrition. Foods and food supply TX341-641 Abraham T. Girgih Ifeanyi D. Nwachukwu Fida Hasan Tayo N. Fagbemi Tom Gill Rotimi E. Aluko Kinetics of the inhibition of renin and angiotensin I-converting enzyme by cod (Gadus morhua) protein hydrolysates and their antihypertensive effects in spontaneously hypertensive rats |
topic_facet |
cod protein hydrolysate angiotensin I-converting enzyme renin enzyme inhibition kinetics IC50 systolic blood pressure spontaneously hypertensive rats Nutrition. Foods and food supply TX341-641 |
description |
Background: Cod muscle has a balanced protein profile that contains potentially bioactive amino acid sequences. However, there is limited information on release of these peptides from the parent proteins and their ability to modulate mammalian blood pressure. Objective: The aim of this study was to generate cod antihypertensive peptides with potent in vitro inhibitory effects against angiotensin-converting enzyme (ACE) and renin. The most active peptides were then tested for systolic blood pressure (SBP)-reducing ability in spontaneously hypertensive rats (SHRs). Design: Cod protein hydrolysate (CPH) was produced by subjecting the muscle proteins to proteolysis first by pepsin and followed by trypsin+chymotrypsin combination. In order to enhance peptide activity, the CPH was subjected to reverse-phase (RP)-HPLC separation to yield four fractions (CF1, CF2, CF3, and CF4). The CPH and RP-HPLC fractions were each tested at 1 mg/mL for ability to inhibit in vitro ACE and renin activities. CPH and the most active RP-HPLC fraction (CF3) were then used for enzyme inhibition kinetics assays followed by oral administration (200 and 30 mg/kg body weight for CPH and CF3, respectively) to SHRs and SBP measurements within 24 h. Results: The CPH, CF3, and CF4 had similar ACE-inhibitory activities of 84, 85, and 87%, which were significantly (p<0.05) higher than the values for CF1 (69%) and CF2 (79%). Conversely, the CF3 had the highest (63%) renin-inhibitory activity (p<0.05) when compared to CPH (43%), CF1 (15%), and CF4 (44%). CPH and CF3 exhibited uncompetitive mode of ACE inhibition, whereas renin inhibition was non-competitive. Even at a 6.7-fold lower dosage, the CF3 significantly (p<0.05) reduced SBP (maximum −40.0 mmHg) better than CPH (maximum −19.1 mmHg). Conclusions: RP-HPLC fractionation led to enhanced antihypertensive effects of cod peptides, which may be due to a stronger renin-inhibitory activity. |
format |
Article in Journal/Newspaper |
author |
Abraham T. Girgih Ifeanyi D. Nwachukwu Fida Hasan Tayo N. Fagbemi Tom Gill Rotimi E. Aluko |
author_facet |
Abraham T. Girgih Ifeanyi D. Nwachukwu Fida Hasan Tayo N. Fagbemi Tom Gill Rotimi E. Aluko |
author_sort |
Abraham T. Girgih |
title |
Kinetics of the inhibition of renin and angiotensin I-converting enzyme by cod (Gadus morhua) protein hydrolysates and their antihypertensive effects in spontaneously hypertensive rats |
title_short |
Kinetics of the inhibition of renin and angiotensin I-converting enzyme by cod (Gadus morhua) protein hydrolysates and their antihypertensive effects in spontaneously hypertensive rats |
title_full |
Kinetics of the inhibition of renin and angiotensin I-converting enzyme by cod (Gadus morhua) protein hydrolysates and their antihypertensive effects in spontaneously hypertensive rats |
title_fullStr |
Kinetics of the inhibition of renin and angiotensin I-converting enzyme by cod (Gadus morhua) protein hydrolysates and their antihypertensive effects in spontaneously hypertensive rats |
title_full_unstemmed |
Kinetics of the inhibition of renin and angiotensin I-converting enzyme by cod (Gadus morhua) protein hydrolysates and their antihypertensive effects in spontaneously hypertensive rats |
title_sort |
kinetics of the inhibition of renin and angiotensin i-converting enzyme by cod (gadus morhua) protein hydrolysates and their antihypertensive effects in spontaneously hypertensive rats |
publisher |
Swedish Nutrition Foundation |
publishDate |
2015 |
url |
https://doi.org/10.3402/fnr.v59.29788 https://doaj.org/article/bd5990fd04e5469297a8ae0506f98631 |
genre |
Gadus morhua |
genre_facet |
Gadus morhua |
op_source |
Food & Nutrition Research, Vol 59, Iss 0, Pp 1-9 (2015) |
op_relation |
http://www.foodandnutritionresearch.net/index.php/fnr/article/view/29788/44348 https://doaj.org/toc/1654-661X 1654-661X doi:10.3402/fnr.v59.29788 https://doaj.org/article/bd5990fd04e5469297a8ae0506f98631 |
op_doi |
https://doi.org/10.3402/fnr.v59.29788 |
container_title |
Food & Nutrition Research |
container_volume |
59 |
container_issue |
1 |
container_start_page |
29788 |
_version_ |
1766005783898619904 |