RESUMO

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.

Assuntos

Lactobacillus acidophilus/enzimologia , Glicoproteínas de Membrana/metabolismo , N-Acetil-Muramil-L-Alanina Amidase/metabolismo , Sequência de Aminoácidos , Bacillus subtilis/enzimologia , Parede Celular/metabolismo , Clonagem Molecular , Dados de Sequência Molecular , Alinhamento de Sequência