Enhancement of solubility in Escherichia coli and purification of an aminotransferase from Sphingopyxis sp. MTA144 for deamination of hydrolyzed fumonisin B1 |
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| Authors: | Doris Hartinger Stefan Heinl Heidi Elisabeth Schwartz Reingard Grabherr Gerd Schatzmayr Dietmar Haltrich Wulf-Dieter Moll |
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| Affiliation: | (1) BIOMIN Research Center, Technopark 1, 3430 Tulln, Austria;(2) Institute of Applied Microbiology, Department of Biotechnology, University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria;(3) Center for Analytical Chemistry, Department for Agrobiotechnology IFA-Tulln, University of Natural Resources and Life Sciences, Vienna, Konrad Lorenz Strasse 20, 3430 Tulln, Austria;(4) Food Biotechnology Laboratory, Department of Food Sciences and Technology, University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria |
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| Abstract: | Background Fumonisin B1 is a cancerogenic mycotoxin produced by Fusarium verticillioides and other fungi. Sphingopyxis sp. MTA144 can degrade fumonisin B1, and a key enzyme in the catabolic pathway is an aminotransferase which removes the C2-amino group from hydrolyzed fumonisin B1. In order to study this aminotransferase with respect to a possible future application in enzymatic fumonisin detoxification, we attempted expression of the corresponding fumI gene in E. coli and purification of the enzyme. Since the aminotransferase initially accumulated in inclusion bodies, we compared the effects of induction level, host strain, expression temperature, solubility enhancers and a fusion partner on enzyme solubility and activity. |
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