Inhibition of microbial enzymes in human dental plaque catalyzing the cleavage of the disaccharides maltose, sucrose and lactose was carried out with the alpha-glucosidase inhibitor, acarbose. The maltases from plaque homogenates were totally inhibited, whereas the inhibition of the invertases varied considerably. With increasing inhibitor concentrations, from 1 mM to 50 mM, the inhibition of the invertases increased. Preincubation for 30 min of the plaque homogenate with inhibitor resulted in a 20% increase of the inhibition of invertase activity. The inhibitor showed non-competitive inhibition of the invertases in the homogenates, whereas the maltases were competitively inhibited. The lactases were not inhibited at all. The invertases from human dental plaque may be alpha-glucosidases and/or beta-fructosidases.