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Optimization of enzyme-assisted extraction and characterization of collagen from Chinese sturgeon (Acipenser sturio Linnaeus) skin

BACKGROUND: Sturgeon (Acipenser sturio Linnaeus) skin contains high amount of nutrients including unsaturated fatty acids and collagen. A pepsin-assisted extraction procedure was developed and optimized for the extraction of collagen from Chinese sturgeon (Acipenser sturio Linnaeus) skins. OBJECTIVE...

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Autores principales: Feng, Weiwei, Zhao, Ting, Zhou, Ye, Li, Fang, Zou, Ye, Bai, Shiqi, Wang, Wei, Yang, Liuqing, Wu, Xiangyang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Medknow Publications & Media Pvt Ltd 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3798137/
https://www.ncbi.nlm.nih.gov/pubmed/24143042
http://dx.doi.org/10.4103/0973-1296.117859
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author Feng, Weiwei
Zhao, Ting
Zhou, Ye
Li, Fang
Zou, Ye
Bai, Shiqi
Wang, Wei
Yang, Liuqing
Wu, Xiangyang
author_facet Feng, Weiwei
Zhao, Ting
Zhou, Ye
Li, Fang
Zou, Ye
Bai, Shiqi
Wang, Wei
Yang, Liuqing
Wu, Xiangyang
author_sort Feng, Weiwei
collection PubMed
description BACKGROUND: Sturgeon (Acipenser sturio Linnaeus) skin contains high amount of nutrients including unsaturated fatty acids and collagen. A pepsin-assisted extraction procedure was developed and optimized for the extraction of collagen from Chinese sturgeon (Acipenser sturio Linnaeus) skins. OBJECTIVE: To determine the optimum conditions with the maximum yield of the pepsin-soluble collagen (PSC) extraction. MATERIALS AND METHODS: The conditions of the extraction were optimized using response surface methodology. The Box–Behnken design was used to evaluate the effects of the three independent variables (extraction time, enzyme concentration, and solid–liquid ratio) on the PSC yield of the sturgeon skin. RESULTS: The optimal conditions were: solid–liquid ratio of 1:11.88, enzyme concentration of 2.42%, and extraction time of 6.45 h. The maximum yield of 86.69% of PSC was obtained under the optimal conditions. This value was not significantly different from the predicted value (87.4%) of the RSM (P < 0.05). CONCLUSION: The results of this study indicated that the production of PSC from sturgeon skin is feasible and beneficial. The patterns of sodium dodecyl sulfate-polyacrylamide gel electrophoretic patterns (SDS-PAGE) indicated that the sturgeon skin contains type I collagen, which is made of α-chain and β-chain. The infrared spectra of the collagens also indicated that pepsin hydrolysis does not affect the secondary structure of collagen, especially triple-helical structure.
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spelling pubmed-37981372013-10-18 Optimization of enzyme-assisted extraction and characterization of collagen from Chinese sturgeon (Acipenser sturio Linnaeus) skin Feng, Weiwei Zhao, Ting Zhou, Ye Li, Fang Zou, Ye Bai, Shiqi Wang, Wei Yang, Liuqing Wu, Xiangyang Pharmacogn Mag Original Article BACKGROUND: Sturgeon (Acipenser sturio Linnaeus) skin contains high amount of nutrients including unsaturated fatty acids and collagen. A pepsin-assisted extraction procedure was developed and optimized for the extraction of collagen from Chinese sturgeon (Acipenser sturio Linnaeus) skins. OBJECTIVE: To determine the optimum conditions with the maximum yield of the pepsin-soluble collagen (PSC) extraction. MATERIALS AND METHODS: The conditions of the extraction were optimized using response surface methodology. The Box–Behnken design was used to evaluate the effects of the three independent variables (extraction time, enzyme concentration, and solid–liquid ratio) on the PSC yield of the sturgeon skin. RESULTS: The optimal conditions were: solid–liquid ratio of 1:11.88, enzyme concentration of 2.42%, and extraction time of 6.45 h. The maximum yield of 86.69% of PSC was obtained under the optimal conditions. This value was not significantly different from the predicted value (87.4%) of the RSM (P < 0.05). CONCLUSION: The results of this study indicated that the production of PSC from sturgeon skin is feasible and beneficial. The patterns of sodium dodecyl sulfate-polyacrylamide gel electrophoretic patterns (SDS-PAGE) indicated that the sturgeon skin contains type I collagen, which is made of α-chain and β-chain. The infrared spectra of the collagens also indicated that pepsin hydrolysis does not affect the secondary structure of collagen, especially triple-helical structure. Medknow Publications & Media Pvt Ltd 2013 /pmc/articles/PMC3798137/ /pubmed/24143042 http://dx.doi.org/10.4103/0973-1296.117859 Text en Copyright: © Pharmacognosy Magazine http://creativecommons.org/licenses/by-nc-sa/3.0 This is an open-access article distributed under the terms of the Creative Commons Attribution-Noncommercial-Share Alike 3.0 Unported, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Original Article
Feng, Weiwei
Zhao, Ting
Zhou, Ye
Li, Fang
Zou, Ye
Bai, Shiqi
Wang, Wei
Yang, Liuqing
Wu, Xiangyang
Optimization of enzyme-assisted extraction and characterization of collagen from Chinese sturgeon (Acipenser sturio Linnaeus) skin
title Optimization of enzyme-assisted extraction and characterization of collagen from Chinese sturgeon (Acipenser sturio Linnaeus) skin
title_full Optimization of enzyme-assisted extraction and characterization of collagen from Chinese sturgeon (Acipenser sturio Linnaeus) skin
title_fullStr Optimization of enzyme-assisted extraction and characterization of collagen from Chinese sturgeon (Acipenser sturio Linnaeus) skin
title_full_unstemmed Optimization of enzyme-assisted extraction and characterization of collagen from Chinese sturgeon (Acipenser sturio Linnaeus) skin
title_short Optimization of enzyme-assisted extraction and characterization of collagen from Chinese sturgeon (Acipenser sturio Linnaeus) skin
title_sort optimization of enzyme-assisted extraction and characterization of collagen from chinese sturgeon (acipenser sturio linnaeus) skin
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3798137/
https://www.ncbi.nlm.nih.gov/pubmed/24143042
http://dx.doi.org/10.4103/0973-1296.117859
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