Partial characterization of collagen from purple sea urchin (Anthocidaris crassispina) test

Summary As part of a study to establish an effective use of underutilized resources, purple sea urchin test collagen was prepared by limited pepsin digestion and characterized. This collagen consisted of two α chains and has a chain composition of (α1)₂α2 heterotrimer. The primary structure of the purple sea urchin collagen is different from that of a mammalian such as porcine. Sea urchin collagen has a denaturation temperature of 28 °C which is about 9 °C lower than that of the porcine skin collagen. The yield of collagen was about 35% on the basis of lyophilized dry weight. As the purple sea urchin has the potential as an alternative source of collagen for use in various fields such as foods, medicine, and cosmetics, it is necessary to improve the denaturation temperature of the sea urchin.