4.6 Article

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

Journal

APPLIED AND ENVIRONMENTAL MICROBIOLOGY
Volume 74, Issue 24, Pages 7824-7827

Publisher

AMER SOC MICROBIOLOGY
DOI: 10.1128/AEM.01712-08

Keywords

-

Funding

  1. Consejo Nacional de Investigaciones Cientificas y Tecnicas (CONICET)
  2. University of Buenos Aires (UBA) in Argentina

Ask authors/readers for more resources

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.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.6
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available