Purification and characterization of type II collagen from chick sternal cartilage

Hui Cao; Shi-Ying Xu

doi:10.1016/j.foodchem.2007.09.022

Purification and characterization of type II collagen from chick sternal cartilage

Food Chem. 2008 May 15;108(2):439-45. doi: 10.1016/j.foodchem.2007.09.022. Epub 2007 Sep 18.

Authors

Hui Cao¹, Shi-Ying Xu²

Affiliations

¹ School of Food Science and Technology, Southern Yangtze University, P.O. Box 98, No. 1800, Lihu Road, Wuxi, 214122 Jiangsu, China.
² School of Food Science and Technology, Southern Yangtze University, P.O. Box 98, No. 1800, Lihu Road, Wuxi, 214122 Jiangsu, China. Electronic address: syxu@sytu.edu.cn.

PMID: 26059120
DOI: 10.1016/j.foodchem.2007.09.022

Abstract

Type II collagen was purified from sternal cartilage of the chick using a combination of pepsin digestion, NaCl precipitation and DEAE-sepharose CL 6B ion exchange chromatography. Pepsin-solubilized type II collagen of higher stability can be obtained with the extraction time of 32h, 0.5% pepsin concentration at 20°C. The purified preparation showed a single peak on RP-HPLC and a single band (α-chain) and its dimers (β-chains) on SDS-PAGE with a subunit Mr of 110kDa. The amino acid composition of the type II collagen derived from chick cartilage was closer to that of reference Sigma-Aldrich type II collagen which contains more imino acid. Analysis by differential scanning calorimetry (DSC) and Fourier transform infrared spectroscopy (FTIR) revealed that type II collagen from chick sternal cartilage retains more intermolecular crosslinks during the purification process. Collagen purified from chick sternal cartilage was typical type II collagen and may find applications in functional foods.

Keywords: Characterization; Purification; Secondary structure; Sternal cartilage; Type II collagen.