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Antioxidant Effect and Functional Properties of Hydrolysates Derived from Egg-White Protein

This study utilized commercially available proteolytic enzymes to prepare egg-white protein hydrolysates (EPHs) with different degrees of hydrolysis. The antioxidant effect and functionalities of the resultant products were then investigated. Treatment with Neutrase yielded the most α-amino groups (...

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Autores principales: Cho, Dae-Yeon, Jo, Kyungae, Cho, So Young, Kim, Jin Man, Lim, Kwangsei, Suh, Hyung Joo, Oh, Sejong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Korean Society for Food Science of Animal Resources 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4597870/
https://www.ncbi.nlm.nih.gov/pubmed/26761178
http://dx.doi.org/10.5851/kosfa.2014.34.3.362
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author Cho, Dae-Yeon
Jo, Kyungae
Cho, So Young
Kim, Jin Man
Lim, Kwangsei
Suh, Hyung Joo
Oh, Sejong
author_facet Cho, Dae-Yeon
Jo, Kyungae
Cho, So Young
Kim, Jin Man
Lim, Kwangsei
Suh, Hyung Joo
Oh, Sejong
author_sort Cho, Dae-Yeon
collection PubMed
description This study utilized commercially available proteolytic enzymes to prepare egg-white protein hydrolysates (EPHs) with different degrees of hydrolysis. The antioxidant effect and functionalities of the resultant products were then investigated. Treatment with Neutrase yielded the most α-amino groups (6.52 mg/mL). Alcalase, Flavourzyme, Protamex, and Ficin showed similar degrees of α-amino group liberation (3.19-3.62 mg/mL). Neutrase treatment also resulted in the highest degree of hydrolysis (23.4%). Alcalase and Ficin treatment resulted in similar degrees of hydrolysis. All hydrolysates, except for the Flavourzyme hydrolysate, had greater radical scavenging activity than the control. The Neutrase hydrolysate showed the highest 2,2-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging activity (IC(50)=3.6mg/mL). Therefore, Neutrase was identified as the optimal enzyme for hydrolyzing egg-white protein to yield antioxidant peptides. During Neutrase hydrolysis, the reaction rate was rapid over the first 4 h, and then subsequently declined. The IC(50) value was lowest after the first hour (2.99 mg/mL). The emulsifying activity index (EAI) of EPH treated with Neutrase decreased, as the pH decreased. The EPH foaming capacity was maximal at pH 3.6, and decreased at an alkaline pH. Digestion resulted in significantly higher 1,1-diphenyl-2-picrylhydrazyl (DPPH) and ABTS radical scavenging activity. The active peptides released from egg-white protein showed antioxidative activities on ABTS and DHHP radical. Thus, this approach may be useful for the preparation of potent antioxidant products.
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spelling pubmed-45978702016-01-04 Antioxidant Effect and Functional Properties of Hydrolysates Derived from Egg-White Protein Cho, Dae-Yeon Jo, Kyungae Cho, So Young Kim, Jin Man Lim, Kwangsei Suh, Hyung Joo Oh, Sejong Korean J Food Sci Anim Resour Article This study utilized commercially available proteolytic enzymes to prepare egg-white protein hydrolysates (EPHs) with different degrees of hydrolysis. The antioxidant effect and functionalities of the resultant products were then investigated. Treatment with Neutrase yielded the most α-amino groups (6.52 mg/mL). Alcalase, Flavourzyme, Protamex, and Ficin showed similar degrees of α-amino group liberation (3.19-3.62 mg/mL). Neutrase treatment also resulted in the highest degree of hydrolysis (23.4%). Alcalase and Ficin treatment resulted in similar degrees of hydrolysis. All hydrolysates, except for the Flavourzyme hydrolysate, had greater radical scavenging activity than the control. The Neutrase hydrolysate showed the highest 2,2-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical scavenging activity (IC(50)=3.6mg/mL). Therefore, Neutrase was identified as the optimal enzyme for hydrolyzing egg-white protein to yield antioxidant peptides. During Neutrase hydrolysis, the reaction rate was rapid over the first 4 h, and then subsequently declined. The IC(50) value was lowest after the first hour (2.99 mg/mL). The emulsifying activity index (EAI) of EPH treated with Neutrase decreased, as the pH decreased. The EPH foaming capacity was maximal at pH 3.6, and decreased at an alkaline pH. Digestion resulted in significantly higher 1,1-diphenyl-2-picrylhydrazyl (DPPH) and ABTS radical scavenging activity. The active peptides released from egg-white protein showed antioxidative activities on ABTS and DHHP radical. Thus, this approach may be useful for the preparation of potent antioxidant products. Korean Society for Food Science of Animal Resources 2014 2014-06-30 /pmc/articles/PMC4597870/ /pubmed/26761178 http://dx.doi.org/10.5851/kosfa.2014.34.3.362 Text en Copyright © 2014, Korean Society for Food Science of Animal Resources http://creativecommons.org/licences/by-nc/4.0 This is an open access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licences/by-nc/4.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Article
Cho, Dae-Yeon
Jo, Kyungae
Cho, So Young
Kim, Jin Man
Lim, Kwangsei
Suh, Hyung Joo
Oh, Sejong
Antioxidant Effect and Functional Properties of Hydrolysates Derived from Egg-White Protein
title Antioxidant Effect and Functional Properties of Hydrolysates Derived from Egg-White Protein
title_full Antioxidant Effect and Functional Properties of Hydrolysates Derived from Egg-White Protein
title_fullStr Antioxidant Effect and Functional Properties of Hydrolysates Derived from Egg-White Protein
title_full_unstemmed Antioxidant Effect and Functional Properties of Hydrolysates Derived from Egg-White Protein
title_short Antioxidant Effect and Functional Properties of Hydrolysates Derived from Egg-White Protein
title_sort antioxidant effect and functional properties of hydrolysates derived from egg-white protein
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4597870/
https://www.ncbi.nlm.nih.gov/pubmed/26761178
http://dx.doi.org/10.5851/kosfa.2014.34.3.362
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