Antioxidant and ACE-Inhibitory Activity of Protein Hydrolysates Produced from Atlantic Sea Cucumber (Cucumaria frondosa)

Atlantic sea cucumber is a benthic marine echinoderm found in Northwest Atlantic waters and is harvested mainly for its body wall. The body wall, along with internal organs and aquaphyrangeal bulb/flower, is a rich source of proteins, where the latter parts are often considered as processing discard...

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Published in:Molecules
Main Authors: Tharindu R. L. Senadheera, Abul Hossain, Deepika Dave, Fereidoon Shahidi
Format: Text
Language:English
Published: Multidisciplinary Digital Publishing Institute 2023
Subjects:
Online Access:https://doi.org/10.3390/molecules28135263
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spelling ftmdpi:oai:mdpi.com:/1420-3049/28/13/5263/ 2023-08-20T04:06:06+02:00 Antioxidant and ACE-Inhibitory Activity of Protein Hydrolysates Produced from Atlantic Sea Cucumber (Cucumaria frondosa) Tharindu R. L. Senadheera Abul Hossain Deepika Dave Fereidoon Shahidi agris 2023-07-07 application/pdf https://doi.org/10.3390/molecules28135263 EN eng Multidisciplinary Digital Publishing Institute https://dx.doi.org/10.3390/molecules28135263 https://creativecommons.org/licenses/by/4.0/ Molecules; Volume 28; Issue 13; Pages: 5263 sea cucumber protein hydrolysate antioxidant activity ACE inhibition LDL cholesterol oxidation DNA scission inhibition Text 2023 ftmdpi https://doi.org/10.3390/molecules28135263 2023-08-01T10:46:42Z Atlantic sea cucumber is a benthic marine echinoderm found in Northwest Atlantic waters and is harvested mainly for its body wall. The body wall, along with internal organs and aquaphyrangeal bulb/flower, is a rich source of proteins, where the latter parts are often considered as processing discards. The objective of this research was to produce protein hydrolysates from sea cucumber tissues (body wall, flower, and internal organs) with bioactive properties associated with antioxidants, DNA and LDL cholesterol oxidation inhibition, and angiotensin-I-converting enzyme (ACE) inhibitory effects. The protein hydrolysates were prepared using food-grade commercial enzymes, namely Alcalase, Corolase, and Flavourzyme, individually and in combination, and found that the combination of enzymes exhibited stronger antioxidant potential than the individual enzymes, as well as their untreated counterparts. Similar trends were also observed for the DNA and LDL cholesterol oxidation inhibition and ACE-inhibitory properties of sea cucumber protein hydrolysates, mainly those that were prepared from the flower. Thus, the findings of this study revealed potential applications of sea cucumber-derived protein hydrolysates in functional foods, nutraceuticals, and dietary supplements, as well as natural therapeutics. Text Cucumaria frondosa Northwest Atlantic MDPI Open Access Publishing Molecules 28 13 5263
institution Open Polar
collection MDPI Open Access Publishing
op_collection_id ftmdpi
language English
topic sea cucumber protein hydrolysate
antioxidant activity
ACE inhibition
LDL cholesterol oxidation
DNA scission inhibition
spellingShingle sea cucumber protein hydrolysate
antioxidant activity
ACE inhibition
LDL cholesterol oxidation
DNA scission inhibition
Tharindu R. L. Senadheera
Abul Hossain
Deepika Dave
Fereidoon Shahidi
Antioxidant and ACE-Inhibitory Activity of Protein Hydrolysates Produced from Atlantic Sea Cucumber (Cucumaria frondosa)
topic_facet sea cucumber protein hydrolysate
antioxidant activity
ACE inhibition
LDL cholesterol oxidation
DNA scission inhibition
description Atlantic sea cucumber is a benthic marine echinoderm found in Northwest Atlantic waters and is harvested mainly for its body wall. The body wall, along with internal organs and aquaphyrangeal bulb/flower, is a rich source of proteins, where the latter parts are often considered as processing discards. The objective of this research was to produce protein hydrolysates from sea cucumber tissues (body wall, flower, and internal organs) with bioactive properties associated with antioxidants, DNA and LDL cholesterol oxidation inhibition, and angiotensin-I-converting enzyme (ACE) inhibitory effects. The protein hydrolysates were prepared using food-grade commercial enzymes, namely Alcalase, Corolase, and Flavourzyme, individually and in combination, and found that the combination of enzymes exhibited stronger antioxidant potential than the individual enzymes, as well as their untreated counterparts. Similar trends were also observed for the DNA and LDL cholesterol oxidation inhibition and ACE-inhibitory properties of sea cucumber protein hydrolysates, mainly those that were prepared from the flower. Thus, the findings of this study revealed potential applications of sea cucumber-derived protein hydrolysates in functional foods, nutraceuticals, and dietary supplements, as well as natural therapeutics.
format Text
author Tharindu R. L. Senadheera
Abul Hossain
Deepika Dave
Fereidoon Shahidi
author_facet Tharindu R. L. Senadheera
Abul Hossain
Deepika Dave
Fereidoon Shahidi
author_sort Tharindu R. L. Senadheera
title Antioxidant and ACE-Inhibitory Activity of Protein Hydrolysates Produced from Atlantic Sea Cucumber (Cucumaria frondosa)
title_short Antioxidant and ACE-Inhibitory Activity of Protein Hydrolysates Produced from Atlantic Sea Cucumber (Cucumaria frondosa)
title_full Antioxidant and ACE-Inhibitory Activity of Protein Hydrolysates Produced from Atlantic Sea Cucumber (Cucumaria frondosa)
title_fullStr Antioxidant and ACE-Inhibitory Activity of Protein Hydrolysates Produced from Atlantic Sea Cucumber (Cucumaria frondosa)
title_full_unstemmed Antioxidant and ACE-Inhibitory Activity of Protein Hydrolysates Produced from Atlantic Sea Cucumber (Cucumaria frondosa)
title_sort antioxidant and ace-inhibitory activity of protein hydrolysates produced from atlantic sea cucumber (cucumaria frondosa)
publisher Multidisciplinary Digital Publishing Institute
publishDate 2023
url https://doi.org/10.3390/molecules28135263
op_coverage agris
genre Cucumaria frondosa
Northwest Atlantic
genre_facet Cucumaria frondosa
Northwest Atlantic
op_source Molecules; Volume 28; Issue 13; Pages: 5263
op_relation https://dx.doi.org/10.3390/molecules28135263
op_rights https://creativecommons.org/licenses/by/4.0/
op_doi https://doi.org/10.3390/molecules28135263
container_title Molecules
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