FOOD SCIENCE ›› 2013, Vol. 34 ›› Issue (23): 41-46.doi: 10.7506/spkx1002-6630-201323010

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Isolation and Characterization of Collagens from the Skin of Sturgeon

YANG Ling1,ZHAO Yan2,LU Liang2,WANG Zhong-wen2,SONG Bao-lei3,WANG Zhan-fang3,WANG Hai-bo1,*   

  1. 1.School of Chemical and Environment Engineering, Wuhan Polytechnic University, Wuhan 430023, China;
    2.School of Food Science and Engineering, Wuhan Polytechnic University, Wuhan 430023, China;
    3. Grain Industry Group of Heibei Province, Shijiazhuang 050800, China
  • Received:2013-07-01 Revised:2013-10-30 Online:2013-12-15 Published:2014-01-03
  • Contact: WANG Hai-bo E-mail:wanghaibo818@hotmail.com

Abstract:

In this study, acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) were extracted from sturgeon skin by the
methods of acid and acid-pepsin. The molecular structures and physicochemical properties of ASC and PSC were determined and
compared with those of bovine Achilles tendon collagen. The results indicated that the ASC and PSC were similar in their amino
acid composition and secondary structures, but they were different from those of bovine Achilles tendon collagen. The denaturation
temperatures for these collagens were determined to be 42.81 ℃ for bovine Achilles tendon collagen, 28.04 ℃ for sturgeon skin
ASC and 28.13 ℃ for sturgeon skin PSC, suggesting an obvious difference in thermostability between sturgeon skin collagen and
bovine Achilles tendon collagen. In the solution state, bovine Achilles tendon collagen could more easily form collagen polymers
and was more resistant to enzymatic hydrolysis than sturgeon skin collagen.

Key words: sturgeon skin, bovine Achilles tendon, collagen, isolation, physicochemical properties

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