Angiotensin I-Converting Enzyme (ACE) Inhibitory Activity and ACE Inhibitory Peptides of Salmon (Salmo salar) Protein Hydrolysates Obtained by Human and Porcine Gastrointestinal Enzymes

The objectives of the present study were two-fold: first, to detect whether salmon protein fractions possess angiotensin I-converting enzyme (ACE) inhibitory properties and whether salmon proteins can release ACE inhibitory peptides during a sequential in vitro hydrolysis (with commercial porcine en...

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Published in:International Journal of Molecular Sciences
Main Authors: Małgorzata Darewicz, Justyna Borawska, Gerd Vegarud, Piotr Minkiewicz, Anna Iwaniak
Format: Text
Language:English
Published: Multidisciplinary Digital Publishing Institute 2014
Subjects:
Online Access:https://doi.org/10.3390/ijms150814077
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spelling ftmdpi:oai:mdpi.com:/1422-0067/15/8/14077/ 2023-08-20T04:09:31+02:00 Angiotensin I-Converting Enzyme (ACE) Inhibitory Activity and ACE Inhibitory Peptides of Salmon (Salmo salar) Protein Hydrolysates Obtained by Human and Porcine Gastrointestinal Enzymes Małgorzata Darewicz Justyna Borawska Gerd Vegarud Piotr Minkiewicz Anna Iwaniak agris 2014-08-13 application/pdf https://doi.org/10.3390/ijms150814077 EN eng Multidisciplinary Digital Publishing Institute Bioactives and Nutraceuticals https://dx.doi.org/10.3390/ijms150814077 https://creativecommons.org/licenses/by/3.0/ International Journal of Molecular Sciences; Volume 15; Issue 8; Pages: 14077-14101 human gastrointestinal enzymes commercial porcine enzymes salmon ACE-inhibitory peptides Text 2014 ftmdpi https://doi.org/10.3390/ijms150814077 2023-07-31T20:38:46Z The objectives of the present study were two-fold: first, to detect whether salmon protein fractions possess angiotensin I-converting enzyme (ACE) inhibitory properties and whether salmon proteins can release ACE inhibitory peptides during a sequential in vitro hydrolysis (with commercial porcine enzymes) and ex vivo digestion (with human gastrointestinal enzymes). Secondly, to evaluate the ACE inhibitory activity of generated hydrolysates. A two-step ex vivo and in vitro model digestion was performed to simulate the human digestion process. Salmon proteins were degraded more efficiently by porcine enzymes than by human gastrointestinal juices and sarcoplasmic proteins were digested/hydrolyzed more easily than myofibrillar proteins. The ex vivo digested myofibrillar and sarcoplasmic duodenal samples showed IC50 values (concentration required to decrease the ACE activity by 50%) of 1.06 and 2.16 mg/mL, respectively. The in vitro hydrolyzed myofibrillar and sarcoplasmic samples showed IC50 values of 0.91 and 1.04 mg/mL, respectively. Based on the results of in silico studies, it was possible to identify 9 peptides of the ex vivo hydrolysates and 7 peptides of the in vitro hydrolysates of salmon proteins of 11 selected peptides. In both types of salmon hydrolysates, ACE-inhibitory peptides IW, IY, TVY and VW were identified. In the in vitro salmon protein hydrolysates an ACE-inhibitory peptides VPW and VY were also detected, while ACE-inhibitory peptides ALPHA, IVY and IWHHT were identified in the hydrolysates generated with ex vivo digestion. In our studies, we documented ACE inhibitory in vitro effects of salmon protein hydrolysates obtained by human and as well as porcine gastrointestinal enzymes. Text Salmo salar MDPI Open Access Publishing International Journal of Molecular Sciences 15 8 14077 14101
institution Open Polar
collection MDPI Open Access Publishing
op_collection_id ftmdpi
language English
topic human gastrointestinal enzymes
commercial porcine enzymes
salmon
ACE-inhibitory peptides
spellingShingle human gastrointestinal enzymes
commercial porcine enzymes
salmon
ACE-inhibitory peptides
Małgorzata Darewicz
Justyna Borawska
Gerd Vegarud
Piotr Minkiewicz
Anna Iwaniak
Angiotensin I-Converting Enzyme (ACE) Inhibitory Activity and ACE Inhibitory Peptides of Salmon (Salmo salar) Protein Hydrolysates Obtained by Human and Porcine Gastrointestinal Enzymes
topic_facet human gastrointestinal enzymes
commercial porcine enzymes
salmon
ACE-inhibitory peptides
description The objectives of the present study were two-fold: first, to detect whether salmon protein fractions possess angiotensin I-converting enzyme (ACE) inhibitory properties and whether salmon proteins can release ACE inhibitory peptides during a sequential in vitro hydrolysis (with commercial porcine enzymes) and ex vivo digestion (with human gastrointestinal enzymes). Secondly, to evaluate the ACE inhibitory activity of generated hydrolysates. A two-step ex vivo and in vitro model digestion was performed to simulate the human digestion process. Salmon proteins were degraded more efficiently by porcine enzymes than by human gastrointestinal juices and sarcoplasmic proteins were digested/hydrolyzed more easily than myofibrillar proteins. The ex vivo digested myofibrillar and sarcoplasmic duodenal samples showed IC50 values (concentration required to decrease the ACE activity by 50%) of 1.06 and 2.16 mg/mL, respectively. The in vitro hydrolyzed myofibrillar and sarcoplasmic samples showed IC50 values of 0.91 and 1.04 mg/mL, respectively. Based on the results of in silico studies, it was possible to identify 9 peptides of the ex vivo hydrolysates and 7 peptides of the in vitro hydrolysates of salmon proteins of 11 selected peptides. In both types of salmon hydrolysates, ACE-inhibitory peptides IW, IY, TVY and VW were identified. In the in vitro salmon protein hydrolysates an ACE-inhibitory peptides VPW and VY were also detected, while ACE-inhibitory peptides ALPHA, IVY and IWHHT were identified in the hydrolysates generated with ex vivo digestion. In our studies, we documented ACE inhibitory in vitro effects of salmon protein hydrolysates obtained by human and as well as porcine gastrointestinal enzymes.
format Text
author Małgorzata Darewicz
Justyna Borawska
Gerd Vegarud
Piotr Minkiewicz
Anna Iwaniak
author_facet Małgorzata Darewicz
Justyna Borawska
Gerd Vegarud
Piotr Minkiewicz
Anna Iwaniak
author_sort Małgorzata Darewicz
title Angiotensin I-Converting Enzyme (ACE) Inhibitory Activity and ACE Inhibitory Peptides of Salmon (Salmo salar) Protein Hydrolysates Obtained by Human and Porcine Gastrointestinal Enzymes
title_short Angiotensin I-Converting Enzyme (ACE) Inhibitory Activity and ACE Inhibitory Peptides of Salmon (Salmo salar) Protein Hydrolysates Obtained by Human and Porcine Gastrointestinal Enzymes
title_full Angiotensin I-Converting Enzyme (ACE) Inhibitory Activity and ACE Inhibitory Peptides of Salmon (Salmo salar) Protein Hydrolysates Obtained by Human and Porcine Gastrointestinal Enzymes
title_fullStr Angiotensin I-Converting Enzyme (ACE) Inhibitory Activity and ACE Inhibitory Peptides of Salmon (Salmo salar) Protein Hydrolysates Obtained by Human and Porcine Gastrointestinal Enzymes
title_full_unstemmed Angiotensin I-Converting Enzyme (ACE) Inhibitory Activity and ACE Inhibitory Peptides of Salmon (Salmo salar) Protein Hydrolysates Obtained by Human and Porcine Gastrointestinal Enzymes
title_sort angiotensin i-converting enzyme (ace) inhibitory activity and ace inhibitory peptides of salmon (salmo salar) protein hydrolysates obtained by human and porcine gastrointestinal enzymes
publisher Multidisciplinary Digital Publishing Institute
publishDate 2014
url https://doi.org/10.3390/ijms150814077
op_coverage agris
genre Salmo salar
genre_facet Salmo salar
op_source International Journal of Molecular Sciences; Volume 15; Issue 8; Pages: 14077-14101
op_relation Bioactives and Nutraceuticals
https://dx.doi.org/10.3390/ijms150814077
op_rights https://creativecommons.org/licenses/by/3.0/
op_doi https://doi.org/10.3390/ijms150814077
container_title International Journal of Molecular Sciences
container_volume 15
container_issue 8
container_start_page 14077
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