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从加利福尼亚刺参(Parastichopus californicus)的皮肤和结缔组织中胃蛋白酶溶解胶原蛋白的纯化和特性研究。

Purification and characterization of pepsin-solubilized collagen from skin and connective tissue of giant red sea cucumber (Parastichopus californicus).

机构信息

College of Food Science and Engineering, Ocean University of China, 5 Yushan Road, Qingdao, Shandong Province 266003, People's Republic of China.

出版信息

J Agric Food Chem. 2010 Jan 27;58(2):1270-4. doi: 10.1021/jf9032415.

Abstract

Pepsin-solubilized collagen (PSC) was extracted from giant red sea cucumbers ( Parastichopus californicus ) and characterized for denaturation temperature (T(d)), maximum transition temperature (T(m)), enzyme-digested peptide maps, and gel-forming capability. SDS-PAGE showed that PSCs from giant red sea cucumber skin and connective tissue were both type I collagens, consisting of three alpha(1) chains of approximately 138 kDa each. The amino acid composition and peptide maps of PSCs digested by V8 protease were different from those of calf skin type I collagen. The T(d) and T(m) are 18.5 and 33.2 degrees C, respectively, for skin PSC and are 17.9 and 32.7 degrees C, respectively, for connective tissue PSC. Both skin and connective tissue PSCs exhibited good gel-forming capability at pH 6.5 and at an ionic strength of 300 mM salt (NaCl). Collagen isolated from giant red sea cucumbers might be used as an alternative to mammalian collagen in the food and pharmaceutical industries.

摘要

从巨型海参(Parastichopus californicus)中提取胃蛋白酶可溶胶原蛋白(PSC),并对其变性温度(T(d))、最大转变温度(T(m))、酶解肽图谱和凝胶形成能力进行了表征。SDS-PAGE 显示,来自巨型海参皮和结缔组织的 PSCs 均为 I 型胶原蛋白,由三个约 138 kDa 的α(1)链组成。用 V8 蛋白酶消化的 PSCs 的氨基酸组成和肽图谱与牛皮 I 型胶原蛋白不同。皮肤 PSC 的 T(d)和 T(m)分别为 18.5 和 33.2°C,结缔组织 PSC 的 T(d)和 T(m)分别为 17.9 和 32.7°C。皮肤和结缔组织 PSCs 在 pH 6.5 和 300 mM 盐(NaCl)离子强度下均具有良好的凝胶形成能力。从巨型海参中分离出的胶原蛋白可能在食品和制药工业中替代哺乳动物胶原蛋白。

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