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The Improvement of The Endogenous Antioxidant Property of Stone Fish (Actinopyga lecanora) Tissue Using Enzymatic Proteolysis
The stone fish (Actinopyga lecanora) ethanolic and methanolic tissue extracts were investigated for total phenolic contents (TPCs) as well as antioxidant activity using 2,2-diphenyl-1-picrylhydrazyl (DPPH(•)) radical scavenging activity and ferric reducing antioxidant power (FRAP) assays. Both extra...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Hindawi Publishing Corporation
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3613057/ https://www.ncbi.nlm.nih.gov/pubmed/23586061 http://dx.doi.org/10.1155/2013/849529 |
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author | Bordbar, Sara Ebrahimpour, Afshin Abdul Hamid, Azizah Abdul Manap, Mohd Yazid Anwar, Farooq Saari, Nazamid |
author_facet | Bordbar, Sara Ebrahimpour, Afshin Abdul Hamid, Azizah Abdul Manap, Mohd Yazid Anwar, Farooq Saari, Nazamid |
author_sort | Bordbar, Sara |
collection | PubMed |
description | The stone fish (Actinopyga lecanora) ethanolic and methanolic tissue extracts were investigated for total phenolic contents (TPCs) as well as antioxidant activity using 2,2-diphenyl-1-picrylhydrazyl (DPPH(•)) radical scavenging activity and ferric reducing antioxidant power (FRAP) assays. Both extracts showed low amount of phenolics (20.33 to 17.03 mg of gallic acid equivalents/100 g dried sample) and moderate antioxidant activity (39% to 34% DPPH(•) radical scavenging activity and 23.95 to 22.30 mmol/100 mL FeSO(4) FRAP value). Enzymatic proteolysis was carried out in order to improve the antioxidant activity using six commercially available proteases under their optimum conditions. The results revealed that the highest increase in antioxidant activity up to 85% was obtained for papain-generated proteolysate, followed by alcalase (77%), trypsin (75%), pepsin (68%), bromelain (68%), and flavourzyme (50%) as measured by DPPH(•) radical scavenging activity, whilst for the FRAP value, the highest increase in the antioxidant activity up to 39.2 mmol/100 mL FeSO(4) was obtained for alcalase-generated proteolysate, followed by papain (29.5 mmol/100 mL FeSO(4)), trypsin (23.2 mmol/100 mL FeSO(4)), flavourzyme (24.7 mmol/100 mL FeSO(4)), bromelain (22.9 mmol/100 mL FeSO(4)), and pepsin (20.8 mmol/100 mL FeSO(4)). It is obvious that proteolysis of stone fish tissue by proteolytic enzymes can considerably enhance its antioxidant activity. |
format | Online Article Text |
id | pubmed-3613057 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
spelling | pubmed-36130572013-04-12 The Improvement of The Endogenous Antioxidant Property of Stone Fish (Actinopyga lecanora) Tissue Using Enzymatic Proteolysis Bordbar, Sara Ebrahimpour, Afshin Abdul Hamid, Azizah Abdul Manap, Mohd Yazid Anwar, Farooq Saari, Nazamid Biomed Res Int Research Article The stone fish (Actinopyga lecanora) ethanolic and methanolic tissue extracts were investigated for total phenolic contents (TPCs) as well as antioxidant activity using 2,2-diphenyl-1-picrylhydrazyl (DPPH(•)) radical scavenging activity and ferric reducing antioxidant power (FRAP) assays. Both extracts showed low amount of phenolics (20.33 to 17.03 mg of gallic acid equivalents/100 g dried sample) and moderate antioxidant activity (39% to 34% DPPH(•) radical scavenging activity and 23.95 to 22.30 mmol/100 mL FeSO(4) FRAP value). Enzymatic proteolysis was carried out in order to improve the antioxidant activity using six commercially available proteases under their optimum conditions. The results revealed that the highest increase in antioxidant activity up to 85% was obtained for papain-generated proteolysate, followed by alcalase (77%), trypsin (75%), pepsin (68%), bromelain (68%), and flavourzyme (50%) as measured by DPPH(•) radical scavenging activity, whilst for the FRAP value, the highest increase in the antioxidant activity up to 39.2 mmol/100 mL FeSO(4) was obtained for alcalase-generated proteolysate, followed by papain (29.5 mmol/100 mL FeSO(4)), trypsin (23.2 mmol/100 mL FeSO(4)), flavourzyme (24.7 mmol/100 mL FeSO(4)), bromelain (22.9 mmol/100 mL FeSO(4)), and pepsin (20.8 mmol/100 mL FeSO(4)). It is obvious that proteolysis of stone fish tissue by proteolytic enzymes can considerably enhance its antioxidant activity. Hindawi Publishing Corporation 2013 2013-02-03 /pmc/articles/PMC3613057/ /pubmed/23586061 http://dx.doi.org/10.1155/2013/849529 Text en Copyright © 2013 Sara Bordbar et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Bordbar, Sara Ebrahimpour, Afshin Abdul Hamid, Azizah Abdul Manap, Mohd Yazid Anwar, Farooq Saari, Nazamid The Improvement of The Endogenous Antioxidant Property of Stone Fish (Actinopyga lecanora) Tissue Using Enzymatic Proteolysis |
title | The Improvement of The Endogenous Antioxidant Property of Stone Fish (Actinopyga lecanora) Tissue Using Enzymatic Proteolysis |
title_full | The Improvement of The Endogenous Antioxidant Property of Stone Fish (Actinopyga lecanora) Tissue Using Enzymatic Proteolysis |
title_fullStr | The Improvement of The Endogenous Antioxidant Property of Stone Fish (Actinopyga lecanora) Tissue Using Enzymatic Proteolysis |
title_full_unstemmed | The Improvement of The Endogenous Antioxidant Property of Stone Fish (Actinopyga lecanora) Tissue Using Enzymatic Proteolysis |
title_short | The Improvement of The Endogenous Antioxidant Property of Stone Fish (Actinopyga lecanora) Tissue Using Enzymatic Proteolysis |
title_sort | improvement of the endogenous antioxidant property of stone fish (actinopyga lecanora) tissue using enzymatic proteolysis |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3613057/ https://www.ncbi.nlm.nih.gov/pubmed/23586061 http://dx.doi.org/10.1155/2013/849529 |
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