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Applied and Environmental Microbiology, January 2007, p. 331-333, Vol. 73, No. 1
0099-2240/07/$08.00+0     doi:10.1128/AEM.01569-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

SHORT REPORT

Trigonopsis variabilis D-Amino Acid Oxidase: Control of Protein Quality and Opportunities for Biocatalysis through Production in Escherichia coli{triangledown} ,{dagger}

Iskandar Dib, Damir Stanzer, and Bernd Nidetzky*

Research Centre Applied Biocatalysis, Petersgasse 14, A-8010 Graz, Austria, c/o Institute of Biotechnology and Biochemical Engineering, Graz University of Technology, Petersgasse 12, A-8010 Graz, Austria

Received 7 July 2006/ Accepted 10 October 2006

Trigonopsis variabilis D-amino acid oxidase accounts for 35% of Escherichia coli protein when added D-methionine suppresses the toxic activity of the recombinant product. Permeabilized E. coli cells are reusable and stabilized enzyme preparations. The purified oxidase lacks the microheterogeneity of the natural enzyme. Oriented immobilization of a chimeric oxidase maintains 80% of the original activity in microparticle-bound enzymes.

* Corresponding author. Mailing address: Institute of Biotechnology and Biochemical Engineering, Graz University of Technology, Petersgasse 12/I, A-8010 Graz, Austria. Phone: 43-316-873-8400. Fax: 43-316-873-8434. E-mail: bernd.nidetzky{at}tugraz.at.

{triangledown} Published ahead of print on 20 October 2006.

{dagger} Supplemental material for this article may be found at http://aem.asm.org/.

Applied and Environmental Microbiology, January 2007, p. 331-333, Vol. 73, No. 1
0099-2240/07/$08.00+0     doi:10.1128/AEM.01569-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.





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