Abstract
Objective: The aim of this study is to produce collagen through the extraction and isolation of porcine skin.Methods: Collagen from porcine skin (Sus scrofa domesticus) was isolated, purified, and characterized. Major amino acid content of collagen (glycine,proline, and hydroxyproline) was determined. Samples were extracted with 0.5 N acetic acid and precipitated with 0.9 M NaCl. Characterization testsincluded those to determine the organoleptic content, pH, Fourier-transform infrared analysis, moisture content, ash content, viscosity, and Masson’strichrome staining on collagen tissue. The collagen was further analyzed using high-performance liquid chromatography using C-18® column anda fluorescence detector at 265 nm and 320 nm, acetic buffer (pH 4.2)–acetonitrile (55:45) as mobile phase, and optimum flow rate of 0.8 mL/min.Results: Our findings indicated that the best method for isolating collagen was with 0.1 M NaOH expressed by average contents of glycine, proline, andhydroxyproline in collagen which were 33.663±0.215%, 12.333±0.128%, and 11.303±0.354%, respectively.Conclusion: Porcine collagen has been successfully obtained with this method.
Highlights
For thousands of years, before oil-based synthetic polymers were discovered, collagen was the dominant organic material used to fabricate shoes, clothes, glue, tape, filaments, surgical sutures, and other necessary items
Materials Pigskin was purchased from the traditional market (Pasar agung, Depok, Indonesia), undenatured collagen-II (Inter Health, Nutraceuticals Incorporated), standard of amino acid glycine, proline, and hydroxyproline (Sigma-Aldrich), fluorenylmethyloxycarbonyl chloride (FMOC-Cl)
Cleansing was initiated by NaOH, which binds to dirt and non-collagen proteins; the porcine skin color became whiter compared with the initial pinkish color before immersion
Summary
Before oil-based synthetic polymers were discovered, collagen was the dominant organic material used to fabricate shoes, clothes, glue, tape, filaments, surgical sutures, and other necessary items. Collagen is considered a beneficial biomaterial because it plays a major role in industrial applications, such as in food, clothing, cosmetics, pharmacy, health, and biomedical industry [1,2,3,4,8]. Collagen is the most abundant protein in animals and humans, which exists as 30% of the total protein in tissues and organs. The high demand for collagen in the food industry is fueled by its high protein concentration and functional characteristics, including its high water absorption capacity, gel and emulsion-forming ability, and stabilization ability. In pharmaceutical and biomedical industries, collagen performs several roles in medicine, protein, and gas transport and acts as a substitute for human skin, blood vessels, and ligaments [2,3]. Since 2010, interest and demand for porcine collagen have increased in the cosmetic and beauty industries because of the benefits of collagen-based face creams and sleeping packs for hydrating skin, maintaining skin moisture, and fading the fine lines caused by aging and drying [3]
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