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Evaluation of Methods of Extraction of Collagen and Its Chemical Properties
Thesis Abstract:
The collagen cantent of pig, beef, goat, and buffalo skins was, determned using the method of acid extrachon, Vognarova, Hill, Neuman, and commercial extraction.
The acid-extracted collagen was characterized and its molecular weight and amino acid composition were determined.
Among the extraction methods studied, Vognarova method yielded the highest collagen content, followed by commercial extraction, Neuman method, Hill method, and acid extraction methods.
The collagen coment of pig skin obtained by acid extraction was 4.5 mg hydroxyproline/5 g fresh weight of sample (equal to 1.6 g collagen/100 g protein), which was lower as compared with the data (7 mg hydroxyproline/5 g fresh weight of simple) obtained by Klein et al. (1969).
In the Vognarova ecxtaction method, the collagen content obtained in pig, beff, goat, and buffalo skins were 46.7, 55.2, 52.6, and 56.3 g/100 g protein, respectively. Meanwhile, the collagen solubilized by Hill extraction method tn pig, beef, goat, and buffalo skins were 15.5, 1.5, 9.6. and 0.6 g/100 g protein, respectively. The collagen solubilized by commercial extraction method in pig, beef, goat, and buffalo skins were 32.8, 30.5, 17.8, and 9.1 g/100 g protein, respectively. In the food grade collagen extraction method. The collagen control obtained in pig, beef, goat, and buffalo skin were 42.1, 48.9, 51.6. and 49.1 g/100 protein, respectively. Meanwhile, the collagen obtained by Neuman extraction method in pig, beef, goat. and buffalo skins were 21.0, 31.1, 27.3, and 31.1 g/100 g proletn, respectively.
The acid-extracted collagen from the skin of the animal species used gave two-protein sub-units. The first and second sub-units of pig skin collagen had molecular weights of 547,000 and 313,300 daltons, respectively. The first and second sub-units of beef skin collagens had molecular weights of 562,300 and 309.700 daltons, respectively, while those of goat skin collogen had molecular weights of 602,500 and 345,100 daltons, respectively. Molecular weights of 559,700 and 353,200 dahons were estimated from first sub-unit and second sub-unit respectively, of buffalo skin collagen.
Glycine content was the highest among the amino acids found in pig skin collagen (23.46%). beef skin collagen (25.83%), goat skin collagen (17.43%), and buffalo skin collagen (19.77%). All the animal skin collagen studied showed that glycine, proline, hydroxyproline, glumatic acid, and alanine were the predominant amino acids present. Animal skin collagen had no Cystine residue.