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作 者:杨霞[1] 王珊珊[1] 赵芙钗[1] 陶宇[1] 李八方[1]
机构地区:[1]中国海洋大学食品科学与工程学院水产加工与贮藏系,山东青岛266003
出 处:《精细化工》2011年第9期883-886,共4页Fine Chemicals
基 金:国家自然科学基金(30871943)~~
摘 要:分别采用酸法和酶法提取驴皮胶原蛋白,并测定了所提取胶原蛋白的性质。结果表明,两种方法提取的胶原蛋白紫外最大吸收峰都在234 nm处,在280 nm处吸收较小;两者红外吸收光谱相似,并且都具有三股螺旋结构;电泳图谱分析所得胶原蛋白的亚基组成形式为(α1)2α2,推测所提取的是Ⅰ型胶原蛋白;DSC(示差量热扫描法)测定发现,酶溶性胶原蛋白的热收缩温度(65.33℃)高于酸溶性胶原蛋白(50.90℃);羟脯氨酸测定发现,酶法提取驴皮胶原蛋白的纯度高于酸法提取驴皮胶原蛋白的纯度。Citric-soluble collagen (CSC) and pepsin-soluble collagen ( PSC ) were successfully extracted from donkey skin, and the properties of the collagens were investigated and compared. The results show that both collagens exhibited a maximum absorbance at 234 nm, but little absorbance near 280 nm. FTIR measurements of CSC and PSC were quite similar, and both demonstrated the existence of triplehelix structure. Based on sodium dodecyl sulfate-polyacrylamide gel electrophoretic (SDS-PAGE) patterns,both samples were identified as type I collagen, containing two different a chains (α1 and α2 ). Nevertheless, DSC (differential scanning calorimetry) detection shows that the thermal transition temperature of PSC ( 65.33℃ ) was slightly higher than that of CSC ( 50. 90℃ ). Hydroxyproline determination shows that the purity of CSC was higher than that of PSC.
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