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Hindawi Publishing Corporation International Journal of Microbiology Volume 2010, Article ID 196363, 7 pages doi:10.1155/2010/196363 Research Article Characterization of the Escherichia coli Antifungal Protein PPEBL21 V. Yadav,1 R. Mandhan,2 M. Kumar,3 J. Gupta,4 and G. L. Sharma3 1 National Institute for Health, Rockville Pike, Bethesda, MD 20892, USA 2 Department of Biotechnology, Kurukshetra University, Kurukshetra 136119, India 3 Institute of Genomics and Integrative Biology, Mall Road, Delhi 110007, India 4 Research Institute of the McGill University Health Centre, Montreal, QC, Canada H3G 1A4 ´ Correspondence should be addressed to G. L. Sharma, drglsharma@ Received 22 December 2009; Accepted 9 March 2010 Academic Editor: Marco Gobbetti Copyright © 2010 V. Yadav et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. An antifungal protein isolated from Escherichia coli BL21 (PPEBL21) and predicted to be alcohol dehydrogenase (ADH) was subjected to biological characterization. The PPEBL21, indeed, demonstrated propionaldehyde-specific ADH activity. The Km and Vmax of PPEBL21 were found to be 644.8 μM and 1.2 U/mg, respectively. In-gel activity assay also showed that PPEBL21 was a propionaldehyde-specific ADH. The pI of PPEBL21 was observed to be 7.8. PPEBL21 was found to be stable up to a temperature of 40◦C with optimum activity at pH 7.5. The decrease in pH decreased the activity of PPEBL21. These results suggested that PPEBL21 having alcohol dehydrogenase activity and stability at significantly high