FOOD SCIENCE ›› 2013, Vol. 34 ›› Issue (9): 24-27.doi: 10.7506/spkx1002-6630-201309006

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Physico-chemical Characteristics of Type Ⅱ Collagen Isolated from Prionace glauca Cartilage

SONG Rui-rui1,2,BAO Bin3,BU Yong-shi1,WANG Yong-xian1,CHEN Li-juan1,WU Wen-hui2,3,*   

  1. 1. College of Food Science and Technology, Shanghai Ocean University, Shanghai 201306, China;
    2. Shanghai Aquatic Products Processing and Storage Engineering Technology Research Center, Shanghai 201306, China;
    3. Institute of Marine Science, Shanghai Ocean University, Shanghai 201306, China
  • Received:2012-05-29 Revised:2013-04-07 Online:2013-05-15 Published:2013-05-07
  • Contact: WU Wen-hui E-mail:whwu@shou.edu.cn

Abstract:

Objective: To isolate type Ⅱ collagen from Prionace glauca cartilage using alkali treatment/pepsin hydrolysis
method, and to determine its biological activity. Methods: The freeze-dried Prionace glauca cartilage was crushed into 60-
200 mesh powder. Then, NaOH treatment and hydrolysis with pepsin were conducted. After salting and dialysis, the type Ⅱ
collagen was obtained. SDS-PAGE, amino acid composition analysis, UV spectroscopic scanning and differential scanning
calorimetry were applied to identify the type Ⅱ collagen. Results: Prionace glauca type Ⅱ collagen was composed of α1
chain and had the molecular weight of 130 kD. Glycine revealed the highest population in Prionace glauca type Ⅱ collagen
with the ratio of 356‰. Meanwhile, type Ⅱ collagen from Prionace glauca was rich in alanine, proline and hydroxyproline.
Moreover, type Ⅱ collagen from Prionace glauca had the characteristics of Gly-X-Y chain, UV absorption peak at
226 nm, thermal denaturation temperature of 41 ℃. Conclusion: Type Ⅱ collagen from Prionace glauca separated by alkali
treatment/enzyme hydrolysis has typical characteristics of type Ⅱ collagen.

Key words: typeⅡ collagen, restriction proteolysis, SDS-PAGE, amino acid analysis, UV spectroscopic analysis

CLC Number: