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Characterization of Invertase Activity from Cariogenic Streptococcus mutans

¹ Department of Microbiology, Northwestern University Medical-Dental Schools, Chicago, Illinois 60611

ABSTRACT

Invertase activity from Streptococcus mutans GS-5 has been partially purified and shown to possess ß-fructofuranosidase specificity. The enzyme has a broad pH optimum between pH 5.5 and 7.5 and exhibits maximal activity at 37 C. Fructose, but not the glucose analogue -methyl-D-glucoside, acts as a competitive inhibitor of the enzyme. None of the common glycolytic intermediates or adenine nucleotides had any significant effect on enzyme activity. A molecular weight of approximately 47,000 was estimated for the enzyme. The enzyme does not appear to be catabolically repressed by glucose nor inducible by sucrose. Higher specific activities of the enzyme are observed in fructose or glucose-grown cells compared to sucrose-grown cells. These results are discussed in terms of the regulation of invertase activity in vivo.

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