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Angiotensin-I-Converting Enzyme Inhibitory Activity of Protein Hydrolysates Generated from the Macroalga Laminaria digitata (Hudson) JV Lamouroux 1813

Seaweeds have a long history of use as both food and medicine, especially in Asian cultures. Moreover, there is growing interest in the use of seaweed ingredients and bioactive compounds in pharmaceutical and nutraceutical products. One ailment that seaweed bioactive compounds may impact is hyperten...

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Autores principales: Purcell, Diane, Packer, Michael A., Hayes, Maria
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9222848/
https://www.ncbi.nlm.nih.gov/pubmed/35741988
http://dx.doi.org/10.3390/foods11121792
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author Purcell, Diane
Packer, Michael A.
Hayes, Maria
author_facet Purcell, Diane
Packer, Michael A.
Hayes, Maria
author_sort Purcell, Diane
collection PubMed
description Seaweeds have a long history of use as both food and medicine, especially in Asian cultures. Moreover, there is growing interest in the use of seaweed ingredients and bioactive compounds in pharmaceutical and nutraceutical products. One ailment that seaweed bioactive compounds may impact is hypertension caused by the enzyme Angiotensin Converting Enzyme 1 (ACE-1; EC 3.4.15.1), found within the Renin-Angiotensin Aldosterone System (RAAS), which causes vasoconstriction of blood vessels, including veins and arteries. The aim of this paper is to generate bioactive peptide containing protein hydrolysates from the brown seaweed Laminaria digitata (Hudson) JV Lamouroux 1813. Proteins were extracted from this seaweed by disrupting the seaweed cell wall using a combination of carbohydrases and proteolytic enzymes. Bioactive peptide containing permeates were generated from L. digitata protein hydrolysates, and both hydrolysates and permeates were screened for their ability to inhibit the enzyme ACE-1. The protein content of the permeate fractions was found to be 23.87% compared to the untreated seaweed, which contained 15.08% protein using LECO analysis. Hydrolysis and filtration resulted in a “white” protein powder, and the protein content of this powder increased by 9% compared to the whole seaweed. The total amino acid (TAA) content of the L. digitata protein permeate was 53.65 g/100 g of the sample, and contains over 32% essential amino acids (EAA). Furthermore, the L. digitata permeate was found to inhibit the ACE-1 enzyme by 75% when compared to the commercial drug Captopril© when assayed at a concentration of 1 mg/mL. The inhibition of ACE-1 (the IC(50) value) of 590 µg/mL for the L. digitata permeate compares well with Captopril©, which had 100% inhibition of ACE-1, with an IC(50) value of 500 µg/mL. This study indicates that there is potential to develop protein powders with ACE-1 inhibitory bioactivities from the brown seaweed L. digitata using enzymatic hydrolysis as a cell disruption and protein extraction/hydrolysate generation procedure.
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spelling pubmed-92228482022-06-24 Angiotensin-I-Converting Enzyme Inhibitory Activity of Protein Hydrolysates Generated from the Macroalga Laminaria digitata (Hudson) JV Lamouroux 1813 Purcell, Diane Packer, Michael A. Hayes, Maria Foods Article Seaweeds have a long history of use as both food and medicine, especially in Asian cultures. Moreover, there is growing interest in the use of seaweed ingredients and bioactive compounds in pharmaceutical and nutraceutical products. One ailment that seaweed bioactive compounds may impact is hypertension caused by the enzyme Angiotensin Converting Enzyme 1 (ACE-1; EC 3.4.15.1), found within the Renin-Angiotensin Aldosterone System (RAAS), which causes vasoconstriction of blood vessels, including veins and arteries. The aim of this paper is to generate bioactive peptide containing protein hydrolysates from the brown seaweed Laminaria digitata (Hudson) JV Lamouroux 1813. Proteins were extracted from this seaweed by disrupting the seaweed cell wall using a combination of carbohydrases and proteolytic enzymes. Bioactive peptide containing permeates were generated from L. digitata protein hydrolysates, and both hydrolysates and permeates were screened for their ability to inhibit the enzyme ACE-1. The protein content of the permeate fractions was found to be 23.87% compared to the untreated seaweed, which contained 15.08% protein using LECO analysis. Hydrolysis and filtration resulted in a “white” protein powder, and the protein content of this powder increased by 9% compared to the whole seaweed. The total amino acid (TAA) content of the L. digitata protein permeate was 53.65 g/100 g of the sample, and contains over 32% essential amino acids (EAA). Furthermore, the L. digitata permeate was found to inhibit the ACE-1 enzyme by 75% when compared to the commercial drug Captopril© when assayed at a concentration of 1 mg/mL. The inhibition of ACE-1 (the IC(50) value) of 590 µg/mL for the L. digitata permeate compares well with Captopril©, which had 100% inhibition of ACE-1, with an IC(50) value of 500 µg/mL. This study indicates that there is potential to develop protein powders with ACE-1 inhibitory bioactivities from the brown seaweed L. digitata using enzymatic hydrolysis as a cell disruption and protein extraction/hydrolysate generation procedure. MDPI 2022-06-17 /pmc/articles/PMC9222848/ /pubmed/35741988 http://dx.doi.org/10.3390/foods11121792 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Purcell, Diane
Packer, Michael A.
Hayes, Maria
Angiotensin-I-Converting Enzyme Inhibitory Activity of Protein Hydrolysates Generated from the Macroalga Laminaria digitata (Hudson) JV Lamouroux 1813
title Angiotensin-I-Converting Enzyme Inhibitory Activity of Protein Hydrolysates Generated from the Macroalga Laminaria digitata (Hudson) JV Lamouroux 1813
title_full Angiotensin-I-Converting Enzyme Inhibitory Activity of Protein Hydrolysates Generated from the Macroalga Laminaria digitata (Hudson) JV Lamouroux 1813
title_fullStr Angiotensin-I-Converting Enzyme Inhibitory Activity of Protein Hydrolysates Generated from the Macroalga Laminaria digitata (Hudson) JV Lamouroux 1813
title_full_unstemmed Angiotensin-I-Converting Enzyme Inhibitory Activity of Protein Hydrolysates Generated from the Macroalga Laminaria digitata (Hudson) JV Lamouroux 1813
title_short Angiotensin-I-Converting Enzyme Inhibitory Activity of Protein Hydrolysates Generated from the Macroalga Laminaria digitata (Hudson) JV Lamouroux 1813
title_sort angiotensin-i-converting enzyme inhibitory activity of protein hydrolysates generated from the macroalga laminaria digitata (hudson) jv lamouroux 1813
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9222848/
https://www.ncbi.nlm.nih.gov/pubmed/35741988
http://dx.doi.org/10.3390/foods11121792
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