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Abstract
Desalting is an important process of bone collagen extraction. In this present study, collagens were prepared from tilapia bone using acetic acid and pepsin. The extracted collagen was partially characterized. Prior to extraction, tilapia bone was desalted by soaking in ethylenediaminetetraacetic acid solution and hydrochloric acid. Thermo-gravimetric analysis, X-ray diffraction, Fourier transform infrared spectroscopy, and scanning electron microscopy were performed to analyze the structural characteristics. The extracted protein was classified as collagen by Fourier transform infrared spectroscopy, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and circular dichroism. Results showed that desalination with HCl was fast, but collagen yield was low. No acid-soluble collagen and only 0.5% pepsin-soluble collagen were obtained from HCl-treated fish bone. By comparison, the yields of acid-soluble collagen and pepsin-soluble collagen from ethylenediaminetetraacetic acid-treated fish bone were 3.5 and 6.0%, respectively. These values were observed higher than those from HCl-treated fish bone. In HCl-treated fish bone, the properties of collagen, such as amino acid composition, denaturation temperature, and molecular weight distribution, were different from those of collagen in ethylenediaminetetraacetic acid-treated fish bone. Collagens extracted from ethylenediaminetetraacetic acid-treated fish bone showed more integrated secondary structure. Therefore, ethylenediaminetetraacetic acid can be used more effectively than HCl to extract collagen from tilapia bone.