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

• Published in: Materials
• Main Authors: Haiyan Ju, Xiuying Liu, Gang Zhang, Dezheng Liu, Yongsheng Yang
• Format: Article in Journal/Newspaper
• Language: English
• Published: MDPI AG 2020
• Subjects: type i collagen fibrils; acid-solubilized method; pepsin-aided extraction; aggregation structure; morphology; Technology; T; Electrical engineering. Electronics. Nuclear engineering; TK1-9971; Engineering (General). Civil engineering (General); TA1-2040; Microscopy; QH201-278.5; Descriptive and experimental mechanics; QC120-168.85; evener
• Online Access: https://doi.org/10.3390/ma13020358; https://doaj.org/article/4faa37d0f6274f8cb347cdd6f449b11e

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.