食品科学 ›› 2013, Vol. 34 ›› Issue (9): 24-27.doi: 10.7506/spkx1002-6630-201309006

• 基础研究 • 上一篇    下一篇

蓝鲨软骨Ⅱ型胶原蛋白的物理化学特性

宋瑞瑞1,2,包 斌3,卜永士1,王永先1,陈丽娟1,吴文惠2,3,*   

  1. 1.上海海洋大学食品学院,上海 201306;2.上海水产品加工与贮藏工程技术研究中心,上海 201306;
    3.上海海洋大学海洋科学研究院,上海 201306
  • 收稿日期:2012-05-29 修回日期:2013-04-07 出版日期:2013-05-15 发布日期:2013-05-07
  • 通讯作者: 吴文惠 E-mail:whwu@shou.edu.cn
  • 基金资助:

    国家“863”计划项目(2011AA09070109);上海市教委重点学科建设项目(J50704)

Physico-chemical Characteristics of Type Ⅱ Collagen Isolated from Prionace glauca Cartilage

SONG Rui-rui1,2,BAO Bin3,BU Yong-shi1,WANG Yong-xian1,CHEN Li-juan1,WU Wen-hui2,3,*   

  1. 1. College of Food Science and Technology, Shanghai Ocean University, Shanghai 201306, China;
    2. Shanghai Aquatic Products Processing and Storage Engineering Technology Research Center, Shanghai 201306, China;
    3. Institute of Marine Science, Shanghai Ocean University, Shanghai 201306, China
  • Received:2012-05-29 Revised:2013-04-07 Online:2013-05-15 Published:2013-05-07
  • Contact: WU Wen-hui E-mail:whwu@shou.edu.cn

摘要:

目的:对采用碱处理-胃酶水解方法分离的蓝鲨软骨Ⅱ型胶原蛋白的物理化学特性进行研究。方法:蓝鲨软骨经冷冻干燥粉碎,顺次用碱处理、胃蛋白酶限制性水解、盐析和透析获得Ⅱ型胶原蛋白。采用SDS-PAGE、氨基酸成分分析、紫外光谱扫描和差示扫描量热法对提取的Ⅱ型胶原蛋白进行鉴定。结果:蓝鲨Ⅱ型胶原蛋白由分子质量为130kD的α1链构成,甘氨酸是蓝鲨Ⅱ型胶原蛋白含量最高的氨基酸为356‰,富含丙氨酸、脯氨酸和羟脯氨酸,且肽链氨基酸残基具有Gly-X-Y的构成特点,蓝鲨Ⅱ型胶原蛋白在226nm波长处有紫外吸收峰,变性温度为41℃。结论:采用碱处理-限制性酶水解分离得到蓝鲨Ⅱ型胶原蛋白,具有Ⅱ型胶原蛋白的典型特征。

关键词: Ⅱ型胶原蛋白, 限制性酶解, SDS-PAGE, 氨基酸分析, 紫外光谱分析

Abstract:

Objective: To isolate type Ⅱ collagen from Prionace glauca cartilage using alkali treatment/pepsin hydrolysis
method, and to determine its biological activity. Methods: The freeze-dried Prionace glauca cartilage was crushed into 60-
200 mesh powder. Then, NaOH treatment and hydrolysis with pepsin were conducted. After salting and dialysis, the type Ⅱ
collagen was obtained. SDS-PAGE, amino acid composition analysis, UV spectroscopic scanning and differential scanning
calorimetry were applied to identify the type Ⅱ collagen. Results: Prionace glauca type Ⅱ collagen was composed of α1
chain and had the molecular weight of 130 kD. Glycine revealed the highest population in Prionace glauca type Ⅱ collagen
with the ratio of 356‰. Meanwhile, type Ⅱ collagen from Prionace glauca was rich in alanine, proline and hydroxyproline.
Moreover, type Ⅱ collagen from Prionace glauca had the characteristics of Gly-X-Y chain, UV absorption peak at
226 nm, thermal denaturation temperature of 41 ℃. Conclusion: Type Ⅱ collagen from Prionace glauca separated by alkali
treatment/enzyme hydrolysis has typical characteristics of type Ⅱ collagen.

Key words: typeⅡ collagen, restriction proteolysis, SDS-PAGE, amino acid analysis, UV spectroscopic analysis

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