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      The extracellular biology of the lactobacilli

      , , , , , ,
      FEMS Microbiology Reviews
      Wiley

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          S Altschul (1990)
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            Peptidoglycan structure and architecture.

            The peptidoglycan (murein) sacculus is a unique and essential structural element in the cell wall of most bacteria. Made of glycan strands cross-linked by short peptides, the sacculus forms a closed, bag-shaped structure surrounding the cytoplasmic membrane. There is a high diversity in the composition and sequence of the peptides in the peptidoglycan from different species. Furthermore, in several species examined, the fine structure of the peptidoglycan significantly varies with the growth conditions. Limited number of biophysical data on the thickness, elasticity and porosity of peptidoglycan are available. The different models for the architecture of peptidoglycan are discussed with respect to structural and physical parameters.
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              Bacteriocins: developing innate immunity for food.

              Bacteriocins are bacterially produced antimicrobial peptides with narrow or broad host ranges. Many bacteriocins are produced by food-grade lactic acid bacteria, a phenomenon which offers food scientists the possibility of directing or preventing the development of specific bacterial species in food. This can be particularly useful in preservation or food safety applications, but also has implications for the development of desirable flora in fermented food. In this sense, bacteriocins can be used to confer a rudimentary form of innate immunity to foodstuffs, helping processors extend their control over the food flora long after manufacture.
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                Author and article information

                Journal
                FEMS Microbiology Reviews
                FEMS Microbiol Rev
                Wiley
                1574-6976
                March 01 2010
                March 2010
                March 2010
                March 01 2010
                : 34
                : 2
                : 199-230
                Article
                10.1111/j.1574-6976.2009.00208.x
                20088967
                8c17db3f-1e90-43ac-9ffc-fc46be9c00ae
                © 2010
                History

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