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Isolation, Purifiction And Characterization Of Collagen From Octopus Areolatus Using Acid Soluble Extraction Method

1337 words - 6 pages

The protein collagen has been sought after for its many industrial and medical applications. Usually collagen is extracted from bovine sources; the search is on to extract it from the vast unutilized marine resources. Acid soluble collagen was isolated from skin, arms and visceral organs of Octopus areolatus. This particular species was found in abundance but commercially unworthy. It is also a popular catch used as fish bait. FTIR analysis show characteristic peak. SDS –PAGE confirmed it as Type I collagen.
Keywords: Acid soluble collagen, Octopus areolatus, SDS-PAGE, FTIR.
Collagen is the most abundant protein found in the animal kingdom. It is the major extracellular protein that serves as a main constituent of many connective tissues and gives cells structure from the outside. It constitute about 20% - 30% of total protein content in mammals (Harkness , 1961) .It is a fibrous structural protein of low immunogenicity. Collagen fibres are in built in tissues of all important organs of the body. It has a great tensile strength and widely distributed in all parts such as cartilage, tendons, ligaments, blood vessels, teeth, cornea (crystalline form) but it is especially concentrated in skin associated tissues and bones.
Collagen as a skin supporting albumen provides proper tension and wetness of the skin and its degradation leads to wrinkles that accompany aging. It is responsible for connectivity, elasticity and firmness of the skin and other tissues. It strengthens blood vessels and play an important role in tissue development.

Because of its wide distribution throughout our body, it represents one of the most abundant naturally occurring proteins on earth. Collagen molecules have remarkably diverse forms and functions.

There are atleast 30 different collagen genes dispersed throughout the human genome. These 30 genes generate proteins that combines in a variety of ways to create more than 20 different types of collagen fibrils. Types I, II and III are the most abundant and form fibrils of similar structure.

The structure of collagen was sorted out by G.N.Ramachandran . The collagen molecule consist of three left handed helical chains coiled around each other to form a right handed super coil . Each left handed helix in collagen has amino acid residues per turn and a pitch of 0.94nm , giving rise of 0.31nm per residue. The strands are bound together primarily by hydrogen bonds between carbonyl and amino groups . Covalent bonds are also involved in some cases ( Harkness ,1966).
Collagen are widely used in food , pharmaceutical ,...


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