Nuclear chemistry

Imino acid

Type I collagen

Amino acid

Biology

Fish <Actinopterygii>

Chromatography

Pepsin

Fishery

Endocrinology

Tuna

Biochemistry

Food science

Hydroxyproline

Extraction (chemistry)

Proline

Enzyme

Isoelectric point

Thunnus

Chemistry

Denaturation (fissile materials)

International Journal of Biological Macromolecules

Fish collagen is gaining immense interest because the use of mammalian collagen is restricted due to disease transmission and religious issues. So, collagen was extracted and characterized from three different parts (skin, scale, and bone) of bigeye tuna using the acid and pepsin extraction methods. The yield of acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) in skin were 13.5 ± 0.6% and 16.7 ± 0.7%, respectively, on a dry basis. The yields of PSC in scale and bone were 4.6 ± 0.3% and 2.6 ± 0.3%, respectively, while ASCs were in negligible amount. All the extracted collagens were type I collagen and a high level of imino acids (227-232/1000 residues) was found in all the extracted collagens. The thermal transition temperature (31.6-33.7 °C) and thermal denaturation temperature (31.1-32.2 °C) were higher than those of many temperate- and cold-water fish collagens. All collagens were highly soluble at acidic pH. The isoelectric points were 6.1, 6.4, 5.4, and 5.5 for skin-ASC, skin-PSC, scale-PSC, and bone-PSC, respectively. Therefore, the high collagen contents, especially in the skin, and higher thermal properties of the extracted collagens suggested that they have great potential for use as an alternate for mammalian collagen.

Characterization of marine derived collagen extracted from the by-products of bigeye tuna (Thunnus obesus)