Study on separation and purification of the transglutaminase

摘要：

　　The transglutaminase was purified through alcohol precipitation,ammonium sulphate precipitation,ultrafiltration,gel layer chromatography,and the purified alkaline was demonstrated to be electrophoretic by SDS-PAGE.Using the activity of alkaline protease as indicators.the purification of transglutaminase was optimized.The results indicated that the enzyme activity of purified transglutaminase was 107.86 U.mg-1,final purification factor was 10.42,Activity recovery factor was 27.3%,The enzyme properties of transglutaminase were also studied,The optimal conditions of transglutaminase were as follows:pH6.0,40℃.After incubation at 40℃ for 2h,the residual activity of the enzyme was ablve 90%,and the enzyme was relatively stable at pH5~7.

关键词： transglutaminase purification enzyme activity

作者: Yan-guo Shi Lei Qian Na Zhang Chun-ran Han Ying Liu Yi-fang Zhang Yong-qiang Ma

作者单位: Key Laboratory of Food Science and Engineering of Heilongjiang Province, Harbin University of Commer Harbin Hi-tech Soybean Food Co.Ltd. Harbin 150078 China

会议类型: 国际会议

会议名称: the Second International Conference on Frontiers of Manufacturing and Design Science(第二届制造与设计科学国际会议(ICFMD 2011))

会议地点: 台湾

会议语种:英文

页码: 443-447

在线出版日期: 2011-12-11（万方平台首次上网日期，不代表论文的发表时间）