Study on Separation and Purification of the Transglutaminase
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.
Dongye Sun, Wen-Pei Sung and Ran Chen
Y. G. Shi et al., "Study on Separation and Purification of the Transglutaminase", Applied Mechanics and Materials, Vols. 121-126, pp. 443-447, 2012