Study on Separation and Purification of the Transglutaminase

Abstract:

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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.

Info:

Periodical:

Edited by:

Dongye Sun, Wen-Pei Sung and Ran Chen

Pages:

443-447

DOI:

10.4028/www.scientific.net/AMM.121-126.443

Citation:

Y. G. Shi et al., "Study on Separation and Purification of the Transglutaminase", Applied Mechanics and Materials, Vols. 121-126, pp. 443-447, 2012

Online since:

October 2011

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$35.00

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