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

被引：38

作者：

Nagai, T ^{[1
]}

Suzuki, N ^{[1
]}

机构：

[1] Natl Fisheries Univ, Dept Food Sci & Technol, Yamaguchi 7596595, Japan

来源：

INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY | 2000年 / 35卷 / 05期

关键词：

amino acid composition; fibrillar collagen; marine invertebrates; underutilized resources;

D O I：

10.1046/j.1365-2621.2000.00406.x

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

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 or chains and has a chain composition of (alpha1)(2)alpha2 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 degreesC which is about 9 degreesC 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.

引用

页码：497 / 501

页数：5

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