ABSTRACT
Collagen is the most abundant structural protein in animals (Muyonga et al., 2004). It is brous in nature and makes up about one-third of the total amount of
proteins in the body. It is an essential component of all body tissues such as the skin, bone, tendons, muscles, cartilage, and blood vessels. Gelatin is a colorless, translucent protein fraction derived from parent protein collagen, which is present in the tendons, ligaments, and tissues of mammals, by partially hydrolyzing the parent protein. Collagen’s molecular structure consists of three polypeptide α-chains that are twisted together to form a triple helix. The distinctive feature of collagen is the regular arrangement of amino acids in each of the three chains of the collagen subunit. The sequence of amino acids is characterized by a repetitive unit of glycine (Gly)-proline (Pro)-X, or Gly-X-hydroxyproline (Hyp), where Gly accounts for one-third of the sequence while X and Y can be any other amino acid residue (Gorham, 1991).
