Abstract
Objective: In this study, collagen isolated from bovine tendon was purified and characterized, and the optimum conditions for analysis of glycine,proline, and hydroxyproline were determined.Methods: The collagen isolation process used 0.1 N NaOH as a pretreatment, 0.5 M acetic acid in the extraction, 0.9 M NaCl in the salting-outstep, centrifugation and dialysis for purification, and freeze-drying as the final step. The characterization of the collagen included analysis of theorganoleptic properties, pH, moisture content, viscosity, and ash content. A Fourier-transform infrared (FTIR) spectroscopy analysis and Casson’strichrome staining were also performed. The collagen was hydrolyzed in 6 N HCl for 24 h and derivatized using 9-fluorenylmethoxycarbonyl chloride.The optimum condition was conducted from the optimal wavelength, selection of mobile phase composition, and flow rate.Results: The average content was 11.867±0.20% for glycine, 33.247±0.20% for proline, and 10.51±0.23% for hydroxyproline. The optimum conditionanalysis for collagen was achieved by high-performance liquid chromatography (HPLC) with a C18® column and a fluorescence detector (excitation:265 nm and emission: 320 nm) with mobile phase acetate buffer (pH 4.2):acetonitrile (55:45), and the flow rate was 0.8 mL/min.Conclusion: The collagen isolated from bovine tendon was obtained at a yield of 0.690%, and the identity was confirmed by FTIR functional groupanalysis and Casson’s trichrome staining. The HPLC conditions using a fluorescence detector for analysis of glycine, proline, and hydroxyprolineconcentrations in the bovine tendon collagen were optimized. The analysis of amino acids gave the average levels of 33.247±0.20% for glycine,11.867±0.20% for proline, and 10.51±0.23% for hydroxyproline.
Highlights
Collagen is a fibrous protein located in the extracellular space and in various connective tissues that account for nearly 30% of the total protein in vertebrate and invertebrate organ tissues [1]
Collagen is indispensable as a raw material in the food, cosmetics, and biomaterials industries, especially those in the health field [2]
Judging from its benefits and uses, collagen has an important role for humans, especially in the health field, so the demand and interest in collagen use are expected to increase
Summary
Collagen is a fibrous protein located in the extracellular space and in various connective tissues that account for nearly 30% of the total protein in vertebrate and invertebrate organ tissues [1]. The main sources of collagen are skin tissue, tendons, cartilage, and bones. The production of collagen in Indonesia is still not optimal. In 2003, Indonesia imported >6200 tons of collagen at approximately US $1/g [3]. Collagen can be produced by isolation from bovine tendon, which is a good source [2]. One-third of the protein mass of bovines is collagen, and the tendons have a fairly high content of 85%. Due to increasing cattle production, there have been several studies on collagen isolation from cow body parts, such as tendons. Collagen isolated from bovine tendon was purified and characterized, and the optimum conditions for analysis of glycine, proline, and hydroxyproline were determined
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