Optimization Of Extraction Conditions And Structural Characterization Of Bovine Tendon Collagen Fibers
Keywords
Beef Tendon, Collagen Fiber, Fiber Bundle, Enzymatic Hydrolysis, Structure
Abstract
Using bovine tendon as raw material, collagen fibers were extracted through acid-enzyme combination method. The extraction rate of collagen fibers and soluble collagen content under different times, pH, and enzyme dosage were compared to obtain the optimal process for extracting collagen fibers. SDS-PAGE electrophoresis, DSC, FT-IR, SEM, and AFM were used to characterize the structure of collagen fibers. The research results show that at 4¡ãC, the optimal conditions for acid-enzyme combined hydrolysis are 40 hours, pH 2.5, and 1.0% enzyme. The collagen fiber obtained under this condition has a high extraction rate, obvious infrared characteristic peaks, large molecular weight and narrow distribution, and a denaturation temperature of 66.7¡ãC; SEM shows that the collagen fiber presents a three-dimensional network structure with uniform pores and a pore diameter of approximately 100-300 ¦Ìm; AFM observation Collagen fibers exist in the form of single fibrils, fiber bundles, etc., and the spacing between light and dark horizontal stripes is 60.35nm. It is believed that collagen fibers with natural triple helix structure have been prepared.
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Original research was done by But Weihua
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