Abstract
Further investigation of the extracellular glucosyltransferase activity of Streptococcus sanguis, strain 804 has revealed several glucosyltransferase enzymes with isoelectric points at pH 7.9, 6.4 and less often at about 4.5. The principal enzyme fraction, Ip 7.9, has been shown to be a pure homogeneous protein moving as a single active band by polyacrylamide gel electrophoresis. The equilibrium of the reaction catalyzed by the glucosyltransferase Ip 7.9 is highly in favour of polysaccharide formation based upon the observed disappearance of sucrose and appearance of reducing sugar. No reversibility of the reaction to form sucrose from fructose and dextran could be demonstrated.
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