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

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Article · Volume 9, Issue 36S · pp. 186–192

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

Weiwei Feng1, Ting Zhao1, Ye Zhou2, Fang Li1, Ye Zou1, Shiqi Bai2, Wei Wang2, Liuqing Yang3, Xiangyang Wu4

  1. 1School of Food and Biological Engineering, China.
  2. 2School of Pharmacy, China.
  3. 3School of Chemistry and Chemical Engineering, China.
  4. 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.

Keywords: Extraction; pepsin-soluble collagen; response surface methodology; sturgeon skin; SDS-PAGE

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