梅花鹿鹿茸胶原的理化特性研究  

Physico-chemical Properties of Sika Deer Antler Collagen

作　　者：赵玉红[1] 金秀明[1] 

机构地区：[1]东北林业大学林学院,黑龙江哈尔滨150040

出　　处：《食品科学》2012年第11期75-78,共4页Food Science

基　　金：黑龙江省教育厅科学技术研究指导项目(11553036)

摘　　要：对胃蛋白酶法在酸性条件下制备的梅花鹿鹿茸胶原的理化性质进行研究。通过紫外扫描(UV)、傅里叶红外光谱(FTIR)、氨基酸组成测定、聚丙烯酰胺凝胶电泳(SDS-PAGE)和示差量热扫描(DSC)等方法对其理化性质进行分析。紫外扫描图谱可知,胶原纯度较高,在230nm波长处有强吸收峰;红外光谱表明其酰胺A、酰胺B、酰胺Ⅰ谱带等主要吸收峰与Ⅰ型胶原标品一致,具有三螺旋结构;凝胶电泳表明鹿茸胶原含有α1、α2和β链,符合Ⅰ型胶原特征;氨基酸分析说明其具有典型胶原的氨基酸组成;示差量热扫描测得其热收缩温度(ts)为84.05℃。梅花鹿鹿茸具有典型的I型胶原的理化特性。The physico-chemical properties of sika deer antler collagen extracted in acidic solution with pepsin were determined using ultraviolet （UV） spectroscopy, Fourier transform infrared （FTIR） spectroscopy, amino acid analyzer, SDS-PAGE and differential scanning calorimetry （DSC）. A typical absorption peak at 230 nm was found in the UV spectrum. The FTIR spectrum showed that the amide A, B and I spectral bands were consistent with those standard type I collagen with threespiral structure. SDS-PAGE results indicated that sika deer antler collagen was composed of one β-chain and two different α-chains （ αl and α2）, which were the characteristics of type I collagen. Amino acid composition analysis revealed the characteristic amino acids of type I collagen. The ts was 84.05 ℃. On the basis of the analysis above, it could be concluded that sika deer antler collagen had typical physico-chemical properties of type I collagen.

关 键 词：梅花鹿鹿茸 胶原 大分子蛋白 结构特性 理化性质 

分 类 号：Q816[生物学—生物工程]