Study on Separation and Purification of the Transglutaminase

Abstract:

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°C.After incubation at 40°C for 2h,the residual activity of the enzyme was ablve 90%,and the enzyme was relatively stable at pH5~7.

• Periodical: Applied Mechanics and Materials (Volumes 121-126)
• Pages: 443-447
• DOI: https://doi.org/10.4028/www.scientific.net/AMM.121-126.443
• Online since: October 2011
• Authors: Yan Guo Shi, Lei Qian, Na Zhang, Chun Ran Han, Ying Liu, Yi Fang Zhang, Yong Qiang Ma
• Keywords: Enzyme Activity, Purification, Transglutaminase

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