Murein hydrolase activity in the surface layer of Lactobacillus acidophilus ATCC 4356

En:

Appl. Environ. Microbiol. 2008;74(24):7824-7827

Fecha:

2008

Formato:

application/pdf

Tipo de documento:

info:eu-repo/semantics/article
info:ar-repo/semantics/artículo
info:eu-repo/semantics/publishedVersion

Descriptores:

Bacilli -  Bacteriology -  Salmonella -  Amino acid sequence -  C-terminal domains -  Cloning and expression -  Enzymatic activities -  Functional verification -  Hydrolase activities

Descripción:

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. Copyright © 2008, American Society for Microbiology. All Rights Reserved.
Fil:Acosta, M.P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Palomino, M.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Allievi, M.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Ruzal, S.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.

Identificador(es):

http://hdl.handle.net/20.500.12110/paper_00992240_v74_n24_p7824_Acosta

Derechos:

info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/2.5/ar