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Applied and Environmental Microbiology, December 2008, p. 7824-7827, Vol. 74, No. 24
0099-2240/08/$08.00+0     doi:10.1128/AEM.01712-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Murein Hydrolase Activity in the Surface Layer of Lactobacillus acidophilus ATCC 4356{triangledown}

Mariano Prado Acosta, María Mercedes Palomino, Mariana C. Allievi, Carmen Sanchez Rivas, and Sandra M. Ruzal*

Departamento de Química Biológica, Facultad Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina

Received 24 July 2008/ Accepted 4 October 2008

We describe a new enzymatic functionality for the surface layer (S-layer) of Lactobacillus acidophilus ATCC 4356, namely, an endopeptidase activity against the cell wall of Salmonella enterica serovar Newport, assayed via zymograms and identified by Western blotting. Based on amino acid sequence comparisons, the hydrolase activity was predicted to be located at the C terminus. Subsequent cloning and expression of the C-terminal domain in Bacillus subtilis resulted in the functional verification of the enzymatic activity.

* Corresponding author. Mailing address: Departamento de Química Biológica, Ciudad Universitaria Pabellón II, 4° piso, (1428) Buenos Aires, Argentina. Phone and fax: 54 11 4576 3342. E-mail: sandra{at}qb.fcen.uba.ar

{triangledown} Published ahead of print on 17 October 2008.

Applied and Environmental Microbiology, December 2008, p. 7824-7827, Vol. 74, No. 24
0099-2240/08/$08.00+0     doi:10.1128/AEM.01712-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

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