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KMID : 1024620160360050665
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Food Science of Animal Resources
2016 Volume.36 No. 5 p.665 ~ p.670
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Isolation and Characterization of Pepsin-soluble Collagens from Bones, Skins, and Tendons in Duck Feet
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Kim Hyun-Wook
Yeo In-Jun
Hwang Ko-Eun
Song Dong-Heon
Kim Yong-Jae
Ham Youn-Kyung
Jeong Tae-Jun
Choi Yun-Sang
Kim Cheon-Jei
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Abstract
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The objectives of this study were conducted to characterize pepsin-soluble collagen (PSC) extracted from bones (PSC-B), skins (PSC-S), and tendons (PSC-T) of duck feet and to determine their thermal and structural properties, for better practical application of each part of duck feet as a novel source for collagen. PSC was extracted from each part of duck feet by using 0.5 M acetic acid containing 5% (w/w) pepsin. Electrophoretic patterns showed that the ratio between α1 and α2 chains, which are subunit polypeptides forming collagen triple helix, was approximately 1:1 in all PSCs of duck feet. PSC-B had slightly higher molecular weights for α1 and α2 chains than PSC-S and PSC-T. From the results of differential scanning calorimetry (DSC), higher onset (beginning point of melting) and peak temperatures (maximum point of curve) were found at PSC-B compared to PSC-S and PSC-T (p<0.05). Fourier transform infrared spectroscopy (FT-IR) presented that PSC-S and PSC-T had similar intermolecular structures and chemical bonds, whereas PSC-B exhibited slight difference in amide A region. Irregular dense sheet-like films linked by random-coiled filaments were observed similarly. Our findings indicate that PSCs of duck feet might be characterized similarly as a mixture of collagen type I and II and suggest that duck feet could be used for collagen extraction without deboning and/or separation processes.
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KEYWORD
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collagen, duck feet, DSC, FT-IR, pepsin
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