蓝鲨软骨Ⅱ型胶原蛋白的物理化学特性  

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

作　　者：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] 

机构地区：[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

出　　处：《食品科学》2013年第9期24-27,共4页Food Science

基　　金：国家"863"计划项目(2011AA09070109);上海市教委重点学科建设项目(J50704)

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。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 60200 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.

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 

分 类 号：TS201.7[轻工技术与工程—食品科学]