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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 glueosyltransferase (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.

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