Abstract

Back ground: Collagen accounts for 25percent of all proteins found in vertebrates. The words "collagen"is created with Greek words "kolla" and "genos," which respectively mean "glue" and "formation." It hasa wide range of biological and pharmacological uses. Pig and cow skins provide the majority of thecollagen. Utilizing animal collagen has been restricted as a result of epidemics of certain animal diseasesincluding foot-and-mouth disease (FMD) and bovine spongiform encephalopathy (BSE) (FMD), whichpose a risk of transmission to humansObjective: The goal of this study is to extract collagen from catfish bone.Material and methods: Catfish (Silurus triostegus) bone was used to extract collagen that has beenpepsinized and acid-solubilized collagen (ASC) (PSC). The extracts' proximate composition (moisture,protein, fat, and ash) was measured, and dry weight was used to compute the yield of ASC and PSC. Themolecular weight of experimental collagen ranged from 97 to 200 KD, according to the SDS-PAGEpattern. In order to identify bone collagen, the Fourier Transform Infrared (FTIR) spectra analysis for theacquired ASC and PSC, as well as the standard collagen (type I, II), was used. Using a scanning electronmicroscope (SEM, the morphological structure of ASC and PSC was revealed), and the diffraction angles(2 θ) of ASC and PSC were determined using X-ray analysis. For quality control, the HPLC techniquewas used to determine the collagen.Rustles: The proximate composition of ASC and PSC bone of catfish. The ASC bone of catfish containedmoisture (75.22%), good amount of protein (16.65%) , fat (2.40%) and ash content (0.28 %), While thePSC bone had slightly lower moisture (68.50%) than ASC, it had higher protein (19.93%), fat (1.825%),and ash (0.58%) levels ,HPLC SEM ,FTIR ,Electrophoresis, X-ray.Conclusion: Fish bone was promising sources for preparing collagen, acid soluble collagen (ASC),pepsin soluble collagen (PSC) were successfully extracted by two methods. The collagen extracted frombone catfish, was of type I collagen, which are composed two α1, one α2 chains, and β chains as shownby SDS-PAGE patterns.

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