Specific inhibition of insoluble glucan synthase (GTF-I) by maillard reaction products from casein and albumins.

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Abstract

The Maillard reaction was done with several proteins and aldoses (glucose, glyceraldehyde, and glycolaldehyde) under both neutral and alkaline conditions. Maillard reaction products (MRP) from αs-casein and albumins (ovalbumin, bovine serum albumin, human serum albumin, and α-lactalbumin) inhibited adhesive insoluble glucan synthesis by glucosyltransferase (GTF) of Streptococcus mutans. The magnitude of the inhibitory activity in MRP from αs-casein and the three aldoses correlated with the reactivity of the aldoses with proteins. The MRP from αs-casein and albumins inhibited GTF-I and did not affect GTF-S, while their original proteins stimulated GTF-I specifically. These results suggest that the inhibitory activity of these MRP may be related to the GTF-I stimulating property of their original proteins.

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Details 詳細情報について

  • CRID
    1390001206463623680
  • NII Article ID
    110006324967
  • NII Book ID
    AA00515312
  • DOI
    10.1271/bbb1961.54.1417
  • COI
    1:CAS:528:DyaK3cXkvFKht7k%3D
  • ISSN
    18811280
    00021369
    http://id.crossref.org/issn/00021369
  • Text Lang
    en
  • Data Source
    • JaLC
    • Crossref
    • CiNii Articles
  • Abstract License Flag
    Disallowed

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