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A simple purification method for a glucosyltransferase complex from Streptococcus mutans OMZ 176 with a high yield
1Department of Oral and Maxillofacial Surgery, Shiga University of Medical Science, Japan.
The International Journal of Biochemistry
|January 1, 1988
Summary
Streptococcus mutans glucosyltransferase was purified, achieving a 15,000-fold increase. The enzyme is a complex of three proteins with distinct molecular weights.
Area of Science:
- Biochemistry
- Microbiology
- Enzymology
Background:
- Streptococcus mutans is a key pathogen in dental caries.
- Glucosyltransferases (GTFs) from S. mutans synthesize extracellular polysaccharides crucial for biofilm formation.
Purpose of the Study:
- To purify and characterize glucosyltransferase from Streptococcus mutans OMZ 176.
- To investigate the molecular nature of the purified enzyme.
Main Methods:
- Enzyme purification using ammonium sulfate fractionation.
- Purification employing gel filtration chromatography.
- Analysis of enzyme components by molecular weight.
Main Results:
- Glucosyltransferase was purified approximately 15,000-fold with a 53% yield.
- The purified enzyme exists as a multienzyme complex.
- The complex comprises three distinct protein components with molecular weights of 158,000, 153,000, and 149,000 Da.
Conclusions:
- The glucosyltransferase from Streptococcus mutans OMZ 176 is a multienzyme complex.
- Understanding the subunit composition may provide insights into cariogenic mechanisms.
