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Effect of the α‐glucosidase inhibitor, acarbose, on disaccharide splitting enzymes in human dental plaque
Author(s) -
FIEHN NILSERIK,
MOE DENNIS
Publication year - 1982
Publication title -
european journal of oral sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.802
H-Index - 93
eISSN - 1600-0722
pISSN - 0909-8836
DOI - 10.1111/j.1600-0722.1982.tb01534.x
Subject(s) - acarbose , glucosidases , invertase , maltose , sucrose , dental plaque , lactose , enzyme , disaccharide , biochemistry , chemistry , non competitive inhibition , glycoside hydrolase , biology , microbiology and biotechnology
– Inhibition of microbial enzymes in human dental plaque catalyzing the deavage of the disaccharides maltose, sucrose and lactose was carried out with the α‐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 increases. Prcincubation of 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 α‐glucosidases and/or β‐fructosidases.