Substrate specificity of hydrolase activity of the primer-dependent glucosyltransferases from Streptococcus sobrinus. |
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Authors: | N Hanada T Takehara |
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Affiliation: | Department of Preventive Dentistry, Kyushu Dental College, Kitakyushu, Japan. |
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Abstract: | Four kinds of glucosyltransferases, P1, P2, P3 and P4, were separately purified from the culture supernatant of Streptococcus sobrinus. Their dependencies on primer were analysed. There were two primer-dependent glucosyltransferases (P3 and P4). In the absence of primer 1,6-alpha-D-glucan, P3 was not able to produce glucan from sucrose. However, P3 showed sucrose hydrolase activity, whereas P4 was still able to produce glucan without primer 1,6-alpha-D-glucan. Consequently, glucosyltransferase activity of P4 was incompletely primer-dependent. Both P3 and P4 showed high substrate specificity for sucrose, failing to use melezitose, raffinose, or stachyose as the substrates. |
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