Metabolism of polysaccharides by the Streptococcus mutants dexB gene product.

Abstract

The Streptococcus mutans dexB gene, a member of the multiple sugar metabolism (msm) operon, encodes an intracellular glucan 1,6-alpha-glucosidase which releases glucose from the non-reducing terminus of alpha-1,6-linked isomaltosaccharides and dextran. Comparison of primary amino acid sequences showed strong homology to Bacillus oligo-1,6-glucosidases and, like these enzymes, DexB was able to release free glucose from the alpha-1,4,6-branch point in panose. This suggested a role for DexB in the metabolism of either starch or intracellular polysaccharide, which contain such branch points. However, purified intracellular polysaccharide from the wild-type S. mutans strain LT11 and a mutant deficient in dexB revealed no substantial differences in the extent of branching as demonstrated by iodine staining spectra and the degree of polymerization. Furthermore, thin layer chromatography of radiolabelled intracellular polysaccharide digested with S. mutans wild-type and mutant cell extracts showed no differences in the products obtained. The involvement of DexB in dietary starch metabolism was investigated using alpha-limit dextrins produced from the action of alpha-amylase on starch. These induced the msm operon, including dexB, and the DexB enzyme was able to act on the alpha-limit dextrins to give further fermentable substrates. The transport system encoded by the msm operon can also transport alpha-limit dextrin. DexB may therefore be important in the metabolism of extracellular starch.