The molecular mass distribution, amino acid composition and radical-scavenging
activity of collagen hydrolysates prepared from collagen isolated from the sea
cucumber Stichopus vastus were investigated. b and a1 chains of the collagen were
successfully hydrolysed by trypsin. The molecular mass distribution of the
hydrolysates ranged from 5 to 25 kDa, and they were rich in glycine, alanine,
glutamate, proline and hydroxyproline residues. The hydrolysates exhibited excellent
radical-scavenging activity. These results indicate that collagen hydrolysates from
S. vastus can be used as a functional ingredient in food and nutraceutical products
