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Comparison of the Structural Characteristics of Native Collagen Fibrils Derived from Bovine Tendons Using Two Different Methods: Modified Acid-Solubilized and Pepsin-Aided Extraction

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School of Chemistry and Chemical Engineering, Hubei Key Laboratory of Biomass Fibers and Eco-dyeing and Finishing, Wuhan Textile University, Wuhan 430073, China
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Hubei Key Laboratory of Power System Design and Test for Electrical Vehicle, Hubei University of Arts and Science, Xiangyang 441053, China
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Authors to whom correspondence should be addressed.
Materials 2020, 13(2), 358; https://doi.org/10.3390/ma13020358
Received: 29 November 2019 / Revised: 30 December 2019 / Accepted: 8 January 2020 / Published: 12 January 2020
Native collagen fibrils (CF) were successfully extracted from bovine tendons using two different methods: modified acid-solubilized extraction for A-CF and pepsin-aided method for P-CF. The yields of A-CF and P-CF were up to 64.91% (±1.07% SD) and 56.78% (±1.22% SD) (dry weight basis), respectively. The analyses of both amino acid composition and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) confirmed that A-CF and P-CF were type I collagen fibrils. Both A-CF and P-CF retained the intact crystallinity and integrity of type I collagen’s natural structure by FTIR spectra, circular dichroism spectroscopy (CD) and X-ray diffraction detection. The aggregation structures of A-CF and P-CF were displayed by UV–Vis. However, A-CF showed more intact aggregation structure than P-CF. Microstructure and D-periodicities of A-CF and P-CF were observed (SEM and TEM). The diameters of A-CF and P-CF are about 386 and 282 nm, respectively. Although both A-CF and P-CF were theoretically concordant with the Schmitt hypothesis, A-CF was of evener thickness and higher integrity in terms of aggregation structure than P-CF. Modified acid-solubilized method provides a potential non-enzyme alternative to extract native collagen fibrils with uniform thickness and integral aggregation structure. View Full-Text
Keywords: type I collagen fibrils; acid-solubilized method; pepsin-aided extraction; aggregation structure; morphology type I collagen fibrils; acid-solubilized method; pepsin-aided extraction; aggregation structure; morphology
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Ju, H.; Liu, X.; Zhang, G.; Liu, D.; Yang, Y. Comparison of the Structural Characteristics of Native Collagen Fibrils Derived from Bovine Tendons Using Two Different Methods: Modified Acid-Solubilized and Pepsin-Aided Extraction. Materials 2020, 13, 358.

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