Funding Information This work was supported by the Bundesministerium für Bildung und Forschung (BMBF) project ‘Genomic Design – Doubling Efficiency by Microbial Genomic Design’ 0313917C.
Secretory production of an FAD cofactor-containing cytosolic enzyme (sorbitol–xylitol oxidase from Streptomyces coelicolor) using the twin-arginine translocation (Tat) pathway of Corynebacterium glutamicum
Article first published online: 20 NOV 2012
© 2012 The Authors. Microbial Biotechnology published by Blackwell Publishing Ltd and Society for Applied Microbiology
This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
Special Issue: The Corynebacterium Cell Factory
Volume 6, Issue 2, pages 202–206, March 2013
Total views since publication: 319
How to Cite
Scheele, S., Oertel, D., Bongaerts, J., Evers, S., Hellmuth, H., Maurer, K.-H., Bott, M. and Freudl, R. (2013), Secretory production of an FAD cofactor-containing cytosolic enzyme (sorbitol–xylitol oxidase from Streptomyces coelicolor) using the twin-arginine translocation (Tat) pathway of Corynebacterium glutamicum. Microbial Biotechnology, 6: 202–206. doi: 10.1111/1751-7915.12005
- Issue published online: 15 FEB 2013
- Article first published online: 20 NOV 2012
- Manuscript Accepted: 13 OCT 2012
- Manuscript Revised: 8 OCT 2012
- Manuscript Received: 12 SEP 2012
- Bundesministerium für Bildung und Forschung (BMBF). Grant Number: 0313917C
Carbohydrate oxidases are biotechnologically interesting enzymes that require a tightly or covalently bound cofactor for activity. Using the industrial workhorse Corynebacterium glutamicum as the expression host, successful secretion of a normally cytosolic FAD cofactor-containing sorbitol–xylitol oxidase from Streptomyces coelicolor was achieved by using the twin-arginine translocation (Tat) protein export machinery for protein translocation across the cytoplasmic membrane. Our results demonstrate for the first time that, also for cofactor-containing proteins, a secretory production strategy is a feasible and promising alternative to conventional intracellular expression strategies.