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Journal of Bacteriology logoLink to Journal of Bacteriology
. 1980 May;142(2):521–526. doi: 10.1128/jb.142.2.521-526.1980

Lambda Receptor in the Outer Membrane of Escherichia coli as a Binding Protein for Maltodextrins and Starch Polysaccharides

Thomas Ferenci 1, Marina Schwentorat 1, Susanne Ullrich 1, Jeannine Vilmart 1
PMCID: PMC294017  PMID: 6445892

Abstract

The starch polysaccharides amylose and amylopectin are not utilized by Escherichia coli, but are bound by the bacteria. The following evidence supports the view that the outer membrane λ receptor protein, a component of the maltose/ maltodextrin transport system is responsible for the binding. (i) Amylose and amylopectin both inhibit the transport of maltose into E. coli. (ii) Both polysaccharides prevent binding of non-utilizable maltodextrins by the intact bacterium, a process previously shown to be dependent on components of the maltose transport system (T. Ferenci, Eur. J. Biochem., in press). (iii) A fluorescent amylopectin derivative, O-(fluoresceinyl thiocarbamoyl)-amylopectin, has been synthesized and shown to bind to E. coli in a reversible, saturable manner. Binding of O-(fluoresceinyl thiocarbamoyl)-amylopectin is absent in mutants lacking the λ receptor, but mutations in any of the other components of the maltose transport system do not affect binding as long as λ receptor is present. (iv) Using the inhibition of λ receptor-dependent O-(fluoresceinyl thiocarbamoyl)-amylopectin binding as an assay, the affinities of the λ receptor for maltodextrins and other sugars have been estimated. The affinity for dextrins increases with increasing degree of polymerization (Kd for maltose, 14 mM; for maltotetraose, 0.3 mM; for maltodecaose, 0.075 mM). Maltose and some other di- and trisaccharides are inhibitory to amylopectin binding, but only at concentrations above 1 mM.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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