The structure analysis of type Ⅱ collagen from sturgeon(<i>Acipenser sinensis</i>)cartilage

CHE Shuai; DU Fen; LIU Chu-yi; LI Ba-fang

Volume 39 Issue 4

Feb. 2018

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Science and Technology of Food Industry > 2018 > 39(4): 60-63.

CHE Shuai, DU Fen, LIU Chu-yi, LI Ba-fang. The structure analysis of type Ⅱ collagen from sturgeon(Acipenser sinensis)cartilage[J]. Science and Technology of Food Industry, 2018, 39(4): 60-63.

Citation:

CHE Shuai, DU Fen, LIU Chu-yi, LI Ba-fang. The structure analysis of type Ⅱ collagen from sturgeon(Acipenser sinensis)cartilage[J]. Science and Technology of Food Industry, 2018, 39(4): 60-63.

Citation:

CHE Shuai, DU Fen, LIU Chu-yi, LI Ba-fang. The structure analysis of type Ⅱ collagen from sturgeon(Acipenser sinensis)cartilage[J]. Science and Technology of Food Industry, 2018, 39(4): 60-63.

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The structure analysis of type Ⅱ collagen from sturgeon(Acipenser sinensis)cartilage

1. Marine Biomedical Research Institute of Qingdao, Qingdao 266000, China;
2. College of Food Science and Engineering of Ocean University of China, Qingdao 266000, China

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Received Date: July 13, 2017
Available Online: December 25, 2020

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Abstract

Abstract

In this paper,the pepsin soluble type Ⅱ collagen(PSCⅡ)was extracted by pepsin from sturgeon(Acipenser sinensis)cartilage and its structure was characterized. The SDS-PAGE result showed that the PSCⅡ possessed two kinds of chains(α1 and β)and the molecular weight was about 110 and 200 ku,respectively. The maximum UV absorption of PSCⅡ was 229 nm and the fourier transform infrared(FTIR)and circular dichrosim(CD)results accorded with the characteristics of type Ⅱ collagen form other species. The amino acid analysis showed glycine was the highest population in PSCⅡ with the ratio of 1/3. Meanwhile,PSCⅡ was rich in alanine and proline. Differential scanning calorimeter(DSC)results showed the thermal denaturation temperature of PSCⅡ was 31.5 ℃. PSCⅡ could be used as a good drug carrier because of its porous structure under scanning electron microscope(SEM).
- Acipenser sinensis,
- cartilage,
- type Ⅱ collagen,
- structure analysis

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