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Food, fibre and pharmaceuticals from animals
RESEARCH ARTICLE

Isolation and characterisation of collagen from elk antler velvet

Do Hun Lee A H , Heeok Hong B H , Gaurav Lodhi A , Sun Hee Cheong A F , Pyo Jam Park A F , Tiejun Hu C , Kim Sangwoo D , Sang Ho Moon E F G and Byong Tae Jeon E F G
+ Author Affiliations
- Author Affiliations

A Department of Biotechnology, Konkuk University, Chungju 380-701, Republic of Korea.

B Department of Medical Science, School of Medicine Konkuk University, Seoul 143-701, Republic of Korea.

C Department of Food Science, Jilin Sino-ROK Institute of Animal Science, Changchun 130600, China.

D National Institute of Animal Science, RDA, Suwon, 441-706, Republic of Korea.

E Division of Food Bioscience, Konkuk University, Chungju 380-701, Republic of Korea.

F Nokyong Research Center, Konkuk University, Chungju 380-701, Republic of Korea.

G Corresponding authors. Email: moon0204@kku.ac.kr; hannokwon@kku.ac.kr

H These authors contributed equally to this work.

Animal Production Science 54(8) 1095-1101 https://doi.org/10.1071/AN13281
Submitted: 3 July 2013  Accepted: 14 October 2013   Published: 17 December 2013

Abstract

Collagen was extracted from the antler velvet of elk (Cervus elaphus). Two types of collagen were prepared namely, acetic acid-soluble collagen and pepsin-soluble collagen. The electrophoretic patterns of both of the collagens showed that they were heterotrimeric, i.e. they consisted of α1α2α3. The total yield of the collagen obtained from the elk antler velvet was 12.1%. Amino acid analysis of the collagen by high-performance liquid chromatography showed that imino acid content such as that of proline and hydroxyproline was high, which might contribute to better visco-elastic properties. The peptide mapping of the collagens showed their similarity with porcine Type I collagen, thereby suggesting that the primary structure of both collagens is identical to that of porcine skin Type I collagen. The thermal denaturation temperature was 37°C, which is comparable to porcine Type I collagen and may also be as a result of high imino acid content.


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