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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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 |
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MDPI Open Access Publishing |
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ftmdpi |
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English |
topic |
human gastrointestinal enzymes commercial porcine enzymes salmon ACE-inhibitory peptides |
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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 |
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15 |
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8 |
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14077 |
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14101 |
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1774722532571611136 |