Animal Production Science Animal Production Science Society
Food, fibre and pharmaceuticals from animals
RESEARCH ARTICLE

Isolation and characterisation of acid- and pepsin-soluble collagen from the skin of Cervus korean TEMMINCK var. mantchuricus Swinhoe

Gaurav Lodhi A , Yon-Suk Kim A , Eun-Kyung Kim B , Jin-Woo Hwang A , Hyung-Sik Won A , Whangi Kim C , Sang-Ho Moon D , Byong-Tae Jeon D and Pyo-Jam Park A D E
+ Author Affiliations
- Author Affiliations

A Department of Biotechnology, Konkuk University, Chungju, 27478, Korea.

B Division of Food Bio Science, College of Biomedical and Health Sciences, Konkuk University, Chungju 27478, Korea.

C Department of Applied Chemistry, Konkuk University, Chungju, 27478, Korea.

D Nokyong Research Centre, Konkuk University, Chungju, 27478, Korea.

E Corresponding author. Email: parkpj@kku.ac.kr

Animal Production Science - https://doi.org/10.1071/AN16143
Submitted: 7 March 2016  Accepted: 8 September 2016   Published online: 20 June 2017

Abstract

Acid-soluble collagen and pepsin-soluble collagen were extracted from the skin of deer, Cervus korean TEMMINCK var. mantchuricus Swinhoe. The two types of collagen were then characterised using sodium dodecyl sulfate–polyacrylamide gel electrophoresis, amino acid composition analysis, peptide hydrolysis patterns, thermal denaturation temperature, differential scanning calorimetry, Fourier transform infrared spectroscopy, and nuclear magnetic resonance imaging. The yield of pepsin-soluble collagen (9.62%) was greater than that of acid-soluble collagen (2.24%), but both types of collagen showed similar electrophoretic patterns with each other and with calf skin collagen. The peptide hydrolysis pattern results suggested that calf skin collagen and pepsin-soluble collagen from deer skin may be similar in terms of their primary structure. The thermal denaturation temperature of acid-soluble collagen and pepsin-soluble collagen were 36.67°C and 36.44°C, respectively, and their melting temperatures were 110°C and 120°C, respectively, which suggest high thermal stability. Fourier transform infrared showed a triple helical structure and nuclear magnetic resonance confirmed the presence of ‘hydration’ water. These results provide a basis for large-scale production and further application as alternatives to other mammalian collagens.

Additional keywords: characterisation, collagen, deer skin, extraction.


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