Partial characterization of collagen from purple sea urchin (Anthocidaris crassispina) test
- 1 October 2000
- journal article
- Published by Oxford University Press (OUP) in International Journal of Food Science & Technology
- Vol. 35 (5) , 497-501
- https://doi.org/10.1046/j.1365-2621.2000.00406.x
Abstract
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.Keywords
This publication has 7 references indexed in Scilit:
- Collagen of edible jellyfish exumbrellaJournal of the Science of Food and Agriculture, 1999
- Collagen of edible jellyfish exumbrellaJournal of the Science of Food and Agriculture, 1999
- Occurrence of fibrillar collagen with structure of (α1)2α2 in the test of sea urchin Asthenosoma ijimaiComparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 1996
- Biochemical and immunological characterization of collagen molecules from echinothurioid sea urchin Asthenosoma ijimaiBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1990
- Characterization of Fish Muscle Type I CollagenJournal of Food Science, 1988
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Amino-acid Composition and Thermal Stability of the Skin Collagen of the Antarctic Ice-fishNature, 1968