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Applied and Environmental Microbiology, December 2005, p. 8974-8977, Vol. 71, No. 12
0099-2240/05/$08.00+0     doi:10.1128/AEM.71.12.8974-8977.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

SHORT REPORT

Heterologous Production of Functional Forms of Rhizopus oryzae Lipase in Escherichia coli

Mirella Di Lorenzo,1,2 Aurelio Hidalgo,1 Michael Haas,3 and Uwe T. Bornscheuer1*

Department of Technical Chemistry and Biotechnology, Institute of Chemistry and Biochemistry, Greifswald University, Greifswald, Germany,1 Department of Chemical Engineering, Federico II University, 80125 Napoli, Italy,2 United States Department of Agriculture, ERRC, ARS, Wyndmoor, Pennsylvania3

Received 17 May 2005/ Accepted 10 September 2005

To date, expression of the lipase from Rhizopus oryzae (ROL) in Escherichia coli always led to the formation of inclusion bodies and inactive protein. However, the production of active ROL and its precursor ProROL in soluble form was achieved when E. coli Origami(DE3) and pET-11d were used as expression systems.

* Corresponding author. Mailing address: Department of Technical Chemistry and Biotechnology, Institute of Chemistry and Biochemistry, Greifswald University, Soldmannstr. 16, D-17487 Greifswald, Germany. Phone: 49 3834 86-4367. Fax: 49 3834 86-80066. E-mail: uwe.bornscheuer{at}uni-greifswald.de.

Applied and Environmental Microbiology, December 2005, p. 8974-8977, Vol. 71, No. 12
0099-2240/05/$08.00+0     doi:10.1128/AEM.71.12.8974-8977.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Di Lorenzo, M., Hidalgo, A., Molina, R., Hermoso, J. A., Pirozzi, D., Bornscheuer, U. T. (2007). Enhancement of the Stability of a Prolipase from Rhizopus oryzae toward Aldehydes by Saturation Mutagenesis. Appl. Environ. Microbiol. 73: 7291-7299 [Abstract] [Full Text]  


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