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Optimization of the Extraction and Stability of Antioxidative Peptides from Mackerel (Pneumatophorus japonicus) Protein
This study optimizes the preparation conditions for mackerel protein hydrolysate (MPH) by response surface methodology (RSM) and investigates the stability of the antioxidant activity of MPHs (<2.5 kDa). The optimal conditions were as follows: enzyme concentration of 1726.85 U/g, pH of 7.00, temp...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Hindawi Publishing Corporation
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5282459/ https://www.ncbi.nlm.nih.gov/pubmed/28194421 http://dx.doi.org/10.1155/2017/6837285 |
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author | Wang, Xueqin Yu, Huahua Xing, Ronge Chen, Xiaolin Liu, Song Li, Pengcheng |
author_facet | Wang, Xueqin Yu, Huahua Xing, Ronge Chen, Xiaolin Liu, Song Li, Pengcheng |
author_sort | Wang, Xueqin |
collection | PubMed |
description | This study optimizes the preparation conditions for mackerel protein hydrolysate (MPH) by response surface methodology (RSM) and investigates the stability of the antioxidant activity of MPHs (<2.5 kDa). The optimal conditions were as follows: enzyme concentration of 1726.85 U/g, pH of 7.00, temperature of 39.55°C, time of 5.5 h, and water/material ratio of 25 : 1, and the maximum DPPH scavenging activity was 79.14%. The MPHs indicated significant cellular antioxidant activity at low concentrations. Furthermore, the temperature and freeze-thaw cycles had little effect on the antioxidative stability while pH had significant effect on the antioxidative stability. In addition, the MPHs were sensitive to the metal ions, such as Fe(2+), Fe(3+), Zn(2+), and Cu(2+). Notably, when the concentrations of Fe(2+) and Fe(3+) were 5 mM, the DPPH scavenging activities were only 1.1% and 0.6%, respectively; furthermore, Cu(2+) at a 5 mM concentration could completely inhibit the DPPH scavenging activity of MPHs. In contrast, K(+) and Mg(2+) had no notable effect on the antioxidant activity of MPHs. These results may provide a scientific basis for the processing and application of MPHs. |
format | Online Article Text |
id | pubmed-5282459 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
spelling | pubmed-52824592017-02-13 Optimization of the Extraction and Stability of Antioxidative Peptides from Mackerel (Pneumatophorus japonicus) Protein Wang, Xueqin Yu, Huahua Xing, Ronge Chen, Xiaolin Liu, Song Li, Pengcheng Biomed Res Int Research Article This study optimizes the preparation conditions for mackerel protein hydrolysate (MPH) by response surface methodology (RSM) and investigates the stability of the antioxidant activity of MPHs (<2.5 kDa). The optimal conditions were as follows: enzyme concentration of 1726.85 U/g, pH of 7.00, temperature of 39.55°C, time of 5.5 h, and water/material ratio of 25 : 1, and the maximum DPPH scavenging activity was 79.14%. The MPHs indicated significant cellular antioxidant activity at low concentrations. Furthermore, the temperature and freeze-thaw cycles had little effect on the antioxidative stability while pH had significant effect on the antioxidative stability. In addition, the MPHs were sensitive to the metal ions, such as Fe(2+), Fe(3+), Zn(2+), and Cu(2+). Notably, when the concentrations of Fe(2+) and Fe(3+) were 5 mM, the DPPH scavenging activities were only 1.1% and 0.6%, respectively; furthermore, Cu(2+) at a 5 mM concentration could completely inhibit the DPPH scavenging activity of MPHs. In contrast, K(+) and Mg(2+) had no notable effect on the antioxidant activity of MPHs. These results may provide a scientific basis for the processing and application of MPHs. Hindawi Publishing Corporation 2017 2017-01-17 /pmc/articles/PMC5282459/ /pubmed/28194421 http://dx.doi.org/10.1155/2017/6837285 Text en Copyright © 2017 Xueqin Wang et al. https://creativecommons.org/licenses/by/4.0/ 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 Wang, Xueqin Yu, Huahua Xing, Ronge Chen, Xiaolin Liu, Song Li, Pengcheng Optimization of the Extraction and Stability of Antioxidative Peptides from Mackerel (Pneumatophorus japonicus) Protein |
title | Optimization of the Extraction and Stability of Antioxidative Peptides from Mackerel (Pneumatophorus japonicus) Protein |
title_full | Optimization of the Extraction and Stability of Antioxidative Peptides from Mackerel (Pneumatophorus japonicus) Protein |
title_fullStr | Optimization of the Extraction and Stability of Antioxidative Peptides from Mackerel (Pneumatophorus japonicus) Protein |
title_full_unstemmed | Optimization of the Extraction and Stability of Antioxidative Peptides from Mackerel (Pneumatophorus japonicus) Protein |
title_short | Optimization of the Extraction and Stability of Antioxidative Peptides from Mackerel (Pneumatophorus japonicus) Protein |
title_sort | optimization of the extraction and stability of antioxidative peptides from mackerel (pneumatophorus japonicus) protein |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5282459/ https://www.ncbi.nlm.nih.gov/pubmed/28194421 http://dx.doi.org/10.1155/2017/6837285 |
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