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α‐amylase activity in supragingival dental plaque in humans
Author(s) -
FIEHN N.E.,
MOE D.
Publication year - 1983
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.1600-0722.1983.tb00831.x
Subject(s) - saliva , dental plaque , amylase , chemistry , enzyme , phosphate buffered saline , enzyme assay , starch , specific activity , bacteria , biochemistry , dentistry , microbiology and biotechnology , chromatography , biology , medicine , genetics
– Supragingival plaque samples were examined for α‐amylase activity before and after cultivation. Amylase activity was determined by disappearance of 14 C‐labeled starch in a phosphate buffer, pH 6.9. In all plaque samples α‐amylase activity was observed. On an average 75% of this activity was soluble, while the rest was bound to various plaque components. Known inhibitors of human α‐amylase inhibited the enzyme activity in the plaque samples almost totally. The electrophoretic patterns of α‐amylases in the plaque and human saliva samples were identical. Bacteria cultivated from the plaque samples showed no or low α‐amylase activity. The results indicated that most of α‐amylase activity in supragingival plaque samples are of salivary origin. The greater part of the enzyme activity is extracellular in the plaque, may be located at the plaque surface, and only a minor part is bound to the cells or to the insoluble components in the plaque.