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Insoluble glucan synthesis by Streptococcus mutans serotype c strains
Infection and Immunity
|November 1, 1983
Summary
Ammonium ions enhance insoluble glucan synthesis by dextransucrase in Streptococcus mutans. This study distinguishes dextransucrase and mutansynthetase enzymes involved in glucan production.
Area of Science:
- Microbiology
- Biochemistry
- Enzymology
Background:
- Streptococcus mutans produces glucans crucial for dental plaque formation.
- Dextransucrase and mutansynthetase are key enzymes in glucan synthesis.
- Understanding their distinct roles is vital for controlling cariogenic biofilms.
Purpose of the Study:
- To purify and characterize dextransucrase and mutansynthetase from Streptococcus mutans GS-5.
- To investigate the influence of ammonium ions on glucan synthesis.
- To differentiate between the two enzymes based on their properties and activity.
Main Methods:
- Enzyme purification using ammonium sulfate precipitation and chromatofocusing.
- Glucan synthesis assays under varying conditions (e.g., presence of ammonium ions, primer).
- Enzyme characterization including molecular weight determination, isoelectric focusing, and antibody cross-reactivity.
Main Results:
- Dextransucrase synthesized water-insoluble glucans in the presence of 1.5 M ammonium sulfate, increasing alpha-1,3 linkages.
- Mutansynthetase synthesized primer-dependent insoluble glucan, with activity decreasing in the presence of ammonium ions.
- Dextransucrase and mutansynthetase were distinguished by higher molecular weight, lower isoelectric point, and lack of antibody cross-reactivity for mutansynthetase.
Conclusions:
- Ammonium ions significantly alter the product profile of dextransucrase towards insoluble glucan synthesis.
- Dextransucrase and mutansynthetase are distinct enzymes with different characteristics and roles in insoluble glucan production.
- These findings contribute to understanding the mechanisms of glucan synthesis by Streptococcus mutans serotype c.