Collagen and the hydrolysates derived from marine resources have a wide range of applications in cosmetic and food industries. In Japan, edible sea cucumber species, Apostichopus japonicus, Stichopus naso Semper, and Cucumaria frondosa, are commercially harvested and contain high amounts of collagens. On the other hand, physicochemical properties and nutritional applications of collagen hydrolysates are dependent on peptide molecular mass distribution, with which functional and physiological attributes vary considerably. The aim of this work is to determine the structure and property of the major collagen in sea cucumber and to estimate peptide molecular mass distribution in the hydrolysate. The pepsin-solubilized collagens were successfully purified from the body walls of three sea cucumber species by a method involving disaggregation with a reductant, alkali treatment and limited pepsin digestion of collagen fibers. The SDS-PAGE containing Urea and anion exchange chromatography showed that the major component of pepsin-solubilized collagen consisted of two different α chains which formed (α1)2α2 heterotrimers, but not (α1)3 homotrimers. The hydrolysates by a protease had a molecular mass distribution of 0.2-1.5kDa and were rich in a few amino acids such as glutamic acid when compared with other collagens. These results suggest that the sea cucumber collagen containing heterotrimers has a variation of the amino acid sequence and the hydrolysates may have suitable properties for use as food materials.

Characterization of pepsin-solubilized collagens and the hydrolysates from sea cucumber species

251st National Meeting (2016)

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