Enzymic activity of salivary amylase when bound to the surface of oral streptococci.
The enzymatic activity of salivary amylase bound to the surface of several species of oral streptococci was determined by the production of acid from starch and by the degradation of maltotetraose to glucose in a coupled, spectrophotometric assay. Most strains able to bind amylase exhibited functional enzyme on their surface and produced acid from the products of amylolytic degradation. These strains were unable to utilise starch in the absence of salivary amylase. Two strains failed to produce acid from starch, despite the presence of functional salivary amylase, because they could not utilise maltose. Strains that could not bind salivary amylase failed to produce acid from starch. In no case was all the bound salivary amylase active, and two strains of Streptococcus mitis which bound amylase did not exhibit any enzyme activity on their cell surface. The ability to bind amylase may confer a survival advantage on oral bacteria which inhabit hosts that consume diets containing starch.
Douglas
C W
CW
Department of Oral Pathology, University of Sheffield, UK.
Heath
J
J
Gwynn
J P
JP
D000143:Acids / Q000378:metabolism; D000327:Adsorption; D000681:Amylases / Q000276:immunology / Q000378:metabolism*; D050260:Carbohydrate Metabolism; D006801:Humans; D012463:Saliva / Q000201:enzymology*; D013291:Streptococcus / Q000378:metabolism*
D000143:Acids; D000681:Amylases