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 sour...
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.
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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문제 정의
However, there has been no literature on the isolation and characterization of collagen extracted from each part of duck feet. Therefore, the objectives of this study were to characterize pepsin- soluble collagen (PSC) extracted from bones, skins, and tendons of duck feet and to determine their thermal and structural properties. The results of this current study will provide detailed information on appropriate application of duck feet collagen to the food, pharmaceutic and cos- metic industries.
대상 데이터
A total of three independent batches were conducted. Analysis of variance was performed on all the variables measured using the general linear model (GLM) proce- dure with using SPSS (SPSS Inc.
이론/모형
Sodium dodecyl sulphate-polyacrylamide gel electro- phoresis (SDS-PAGE) was performed by the method of Laemmli (1970), using 7.5% running gels and 5% stack- ing gels (20 μL loaded). PSC (5 mg/mL of protein con- centration) was dissolved in a buffer solution (0.
성능/효과
0 could signify the existence of alpha triple helix structure in collagen molecules. Thus, our results indicate that PSC-S and PSC- T have similar intermolecular cross-links and chemical bonds and suggest that PSC-B had slightly different inter- molecular bindings, which might be affected by the pres- ence of more hydrogen bonds compared to PSC-S and PSC-T.
후속연구
Therefore, the objectives of this study were to characterize pepsin- soluble collagen (PSC) extracted from bones, skins, and tendons of duck feet and to determine their thermal and structural properties. The results of this current study will provide detailed information on appropriate application of duck feet collagen to the food, pharmaceutic and cos- metic industries.
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