【作者】 叶韬； 林琳； 叶应旺； 张晓霞； 姜绍通； 陆剑锋；

【Author】 YE Tao,LIN Lin,YE Yingwang,JIANG Shaotong,Zhang Xiaoxia,LU Jianfeng*(College of Biotechnology and Food Engineering,Hefei University of Technology,Hefei,230009,China)

【机构】 合肥工业大学生物与食品工程学院；

【摘要】 为充分利用鱼片加工废弃物中的胶原蛋白,采用单因素以及正交实验法,研究胃蛋白酶提取罗非鱼胶原蛋白的最佳工艺,精制后的胶原蛋白采用SDS-PAGE电泳、紫外及傅立叶变换红外扫描,圆二色检测,氨基酸分析,热变性温度测定等方法分析胶原蛋白的理化性质。结果显示:乳酸溶液pH 2.6,温度30℃,料液比1:30(g/ml),加酶量200 U/g,提取时间24 h,此工艺条件下的胶原蛋白提取率达到72.2%;所得的胶原蛋白含有2条α链和1条β链,属于典型的I型胶原蛋白;罗非胶原蛋白的主要氨基酸为甘氨酸,脯氨酸,羟脯氨酸,谷氨酸和丙氨酸;罗非鱼胶原蛋白的热变性温度为34.5℃。研究表明,采用胃蛋白酶提取胶原蛋白,提取率和纯度均较高。更多还原

【Abstract】 Fish bone with plenty of collagen is the main offal from fish fillet processing.The collagen from Tilapia(Oreochromis Niloticus) bone after removing impurities was extracted by pepsin digestion under acid condition.The effects of extraction medium,temperature,material to liquid ratio,pepsin addition,extraction duration on yield of collagen were investigated.The optimum conditions using lactic acid as transmitter to extract collagen were pH 2.6,material to liquid ratio(w/v) 1:30,30℃,200U/g pepsin addition,extraction time 24h,and the yield of extracted collagen reached 72.2%.Then,the extracted crude collagen was further purified and its physicochemical property was determined by the methods of SDS-PAGE,UV and FT-IR scanning,DSC,CD and amino acid analysis.The results indicated that the extracted bone collagen was of high purity and belonged to typical collagenⅠ with two α and one β chains.Furthermore,the bone collagen of Tilapia contains high percentages of Gly,Pro,Hyp,Glu and Ala and its denaturation temperature was 34.5℃.更多还原