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Antihypertensive properties of tilapia (Oreochromis spp.) frame and skin enzymatic protein hydrolysates

Proteins from tilapia frame and skin can potentially be precursors of antihypertensive peptides according to the result of BIOPEP analyses. The aim was to generate peptides with inhibitory effects against angiotensin-converting enzyme (ACE) and renin from tilapia frame and skin protein isolates (FPI...

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Autores principales: Lin, Hsin-Chieh, Alashi, Adeola M., Aluko, Rotimi E., Sun Pan, Bonnie, Chang, Yu-Wei
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5678373/
https://www.ncbi.nlm.nih.gov/pubmed/29151830
http://dx.doi.org/10.1080/16546628.2017.1391666
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author Lin, Hsin-Chieh
Alashi, Adeola M.
Aluko, Rotimi E.
Sun Pan, Bonnie
Chang, Yu-Wei
author_facet Lin, Hsin-Chieh
Alashi, Adeola M.
Aluko, Rotimi E.
Sun Pan, Bonnie
Chang, Yu-Wei
author_sort Lin, Hsin-Chieh
collection PubMed
description Proteins from tilapia frame and skin can potentially be precursors of antihypertensive peptides according to the result of BIOPEP analyses. The aim was to generate peptides with inhibitory effects against angiotensin-converting enzyme (ACE) and renin from tilapia frame and skin protein isolates (FPI and SPI). The most active hydrolysate was then tested for blood pressure-lowering ability in spontaneously hypertensive rats (SHRs). Tilapia frame and skin protein hydrolysates (FPHs and SPHs) were respectively produced from FPI and SPI hydrolysis using pepsin, papain, or bromelain. The ACE-inhibitory activities of tilapia protein hydrolysates with varying degree of hydrolysis (DH) were evaluated. In order to enhance the activity, the hydrolysate was fractionated into four fractions (<1 kDa, 1–3 kDa, 3–5 kDa, and 5–10 kDa) and the one with the greatest ability to inhibit in vitro ACE and renin activities was subjected to oral administration (100 mg/kg body weight) to SHRs. Systolic and diastolic blood pressure (SBP and DBP), mean arterial pressure (MAP), and heart rates (HR) were subsequently measured within 24 h. The pepsin-hydrolyzed FPH (FPHPe) with the highest DH (23%) possessed the strongest ACE-inhibitory activity (IC(50): 0.57 mg/mL). Its <1 kDa ultrafiltration fraction (FPHPe1) suppressed both ACE (IC(50): 0.41 mg/mL) and renin activities more effectively than larger peptides. In addition, FPHPe1 significantly (p < 0.05) reduced SBP (maximum −33 mmHg), DBP (maximum −24 mmHg), MAP (maximum −28 mmHg), and HR (maximum −58 beats) in SHRs. FPHPe1 showed both in vitro and in vivo antihypertensive effects, which suggest tilapia processing coproducts may be valuable protein raw materials for producing antihypertensive peptides.
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spelling pubmed-56783732017-11-17 Antihypertensive properties of tilapia (Oreochromis spp.) frame and skin enzymatic protein hydrolysates Lin, Hsin-Chieh Alashi, Adeola M. Aluko, Rotimi E. Sun Pan, Bonnie Chang, Yu-Wei Food Nutr Res Original Article Proteins from tilapia frame and skin can potentially be precursors of antihypertensive peptides according to the result of BIOPEP analyses. The aim was to generate peptides with inhibitory effects against angiotensin-converting enzyme (ACE) and renin from tilapia frame and skin protein isolates (FPI and SPI). The most active hydrolysate was then tested for blood pressure-lowering ability in spontaneously hypertensive rats (SHRs). Tilapia frame and skin protein hydrolysates (FPHs and SPHs) were respectively produced from FPI and SPI hydrolysis using pepsin, papain, or bromelain. The ACE-inhibitory activities of tilapia protein hydrolysates with varying degree of hydrolysis (DH) were evaluated. In order to enhance the activity, the hydrolysate was fractionated into four fractions (<1 kDa, 1–3 kDa, 3–5 kDa, and 5–10 kDa) and the one with the greatest ability to inhibit in vitro ACE and renin activities was subjected to oral administration (100 mg/kg body weight) to SHRs. Systolic and diastolic blood pressure (SBP and DBP), mean arterial pressure (MAP), and heart rates (HR) were subsequently measured within 24 h. The pepsin-hydrolyzed FPH (FPHPe) with the highest DH (23%) possessed the strongest ACE-inhibitory activity (IC(50): 0.57 mg/mL). Its <1 kDa ultrafiltration fraction (FPHPe1) suppressed both ACE (IC(50): 0.41 mg/mL) and renin activities more effectively than larger peptides. In addition, FPHPe1 significantly (p < 0.05) reduced SBP (maximum −33 mmHg), DBP (maximum −24 mmHg), MAP (maximum −28 mmHg), and HR (maximum −58 beats) in SHRs. FPHPe1 showed both in vitro and in vivo antihypertensive effects, which suggest tilapia processing coproducts may be valuable protein raw materials for producing antihypertensive peptides. Taylor & Francis 2017-10-24 /pmc/articles/PMC5678373/ /pubmed/29151830 http://dx.doi.org/10.1080/16546628.2017.1391666 Text en © 2017 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group. http://creativecommons.org/licenses/by/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Original Article
Lin, Hsin-Chieh
Alashi, Adeola M.
Aluko, Rotimi E.
Sun Pan, Bonnie
Chang, Yu-Wei
Antihypertensive properties of tilapia (Oreochromis spp.) frame and skin enzymatic protein hydrolysates
title Antihypertensive properties of tilapia (Oreochromis spp.) frame and skin enzymatic protein hydrolysates
title_full Antihypertensive properties of tilapia (Oreochromis spp.) frame and skin enzymatic protein hydrolysates
title_fullStr Antihypertensive properties of tilapia (Oreochromis spp.) frame and skin enzymatic protein hydrolysates
title_full_unstemmed Antihypertensive properties of tilapia (Oreochromis spp.) frame and skin enzymatic protein hydrolysates
title_short Antihypertensive properties of tilapia (Oreochromis spp.) frame and skin enzymatic protein hydrolysates
title_sort antihypertensive properties of tilapia (oreochromis spp.) frame and skin enzymatic protein hydrolysates
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5678373/
https://www.ncbi.nlm.nih.gov/pubmed/29151830
http://dx.doi.org/10.1080/16546628.2017.1391666
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