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

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Abstract
Pharmacognosy Magazine,2013,9,36s,s32-s37.
Published:September 2013
Type:Original Article
Authors:
Author(s) affiliations:

Weiwei Feng1, Ting Zhao1, Ye Zhou2, Fang Li1, Ye Zou1, Shiqi Bai2, Wei Wang2, Liuqing Yang3, Xiangyang Wu4
1School of Food and Biological Engineering, Jiangsu University, 301 Xuefu Rd., 212013 Zhenjiang, Jiangsu, China
2School of Pharmacy, Jiangsu University, 301 Xuefu Rd., 212013 Zhenjiang, Jiangsu, China
3School of Chemistry and Chemical Engineering, Jiangsu University, 301 Xuefu Rd., 212013 Zhenjiang, Jiangsu, China
4School of Environment, Jiangsu University, 301 Xuefu Rd., 212013 Zhenjiang, Jiangsu, China

Abstract:

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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