Results 111 to 120 of about 691 (143)
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Modelling of oligosaccharide synthesis by dextransucrase
Biotechnology and Bioengineering, 1999Dextransucrase catalyses the formation of dextran, but also of numerous oligosaccharides from sucrose and different acceptors, if appropriate conditions are chosen. Much experimental work has been carried out and a scheme of reactions and a mathematical model have been developed to describe the complex kinetic behaviour of the enzyme.
B, Demuth, H J, Jördening, K, Buchholz
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High pressure enzyme kinetics of dextransucrase
Biophysical Chemistry, 1976The pressure dependence of enzymatic dextran formation has been observed up to 1000 at for several substrate concentrations. First order denaturation effects could be separated from the thermodynamic effects, which lead to a volume of 30.4 to 44.0 ccm per mole for the formation and -13.6ccm per mole for the activation of the enzyme-substrate complex ...
K O, Greulich, H, Ludwig
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Dextransucrase: Studies on donor substrate specificity
Archives of Biochemistry and Biophysics, 1981Abstract Previous studies (D. S. Genghoff and E. J. Hehre, Proc. Soc. Exp. Biol. Med., 1972, 140, 1298–1301) have shown that an α-linked fluorine atom at C-1 of glucose provided sufficient activation to permit this analog to be a donor substrate for dextransucrase. In order to study the specificity at the donor substrate binding site, a series of α-1-
T J, Grier, R M, Mayer
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Interaction of deoxyhalosucrose derivatives with dextransucrase
Carbohydrate Research, 1985Members of a series of deoxyhalosucrose analogs substituted at one, two, or three primary carbon atoms with bromine or chlorine were prepared. Dextransucrase isolated from Streptococcus sanguis was separately treated with 6-bromo-6-deoxysucrose, 6,6'-dibromo-6,6'-dideoxysucrose, 6,1',6'-tribromotrideoxysucrose, and 6,6'-dichlorodideoxysucrose, in order
M K, Bhattacharjee, R M, Mayer
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Streptococcus mutans Dextransucrase: A Review
1978Publisher Summary Two factors contribute to the cariogenic potential of Streptococcus mutans ( S. mutuns). These factors include its ability to produce high yields of lactic acid from a variety of carbon sources and its ability to adhere to hard surfaces by the action of its extracellular polysaccharides. S.
T J, Montville +2 more
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Dextransucrase and the mechanism for dextran biosynthesis
Carbohydrate Research, 2008Remaud-Simeon and co-workers [Moulis, C.; Joucla, G.; Harrison, D.; Fabre, E.; Potocki-Veronese, G.; Monsan, P.; Remaud-Simeon, M. J. Biol. Chem., 2006, 281, 31254-31267] have recently proposed that a truncated Escherichia coli recombinant B-512F dextransucrase uses sucrose and the hydrolysis product of sucrose, D-glucose, as initiator primers for the ...
John F, Robyt +2 more
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TEMPERATURE-SENSITIVE DEXTRANSUCRASE SYNTHESIS BY A LACTOBACILLUS
Journal of Bacteriology, 1963Dunican , L. K. (Cornell University, Ithaca, New York), and H. W. Seeley, Jr. Temperature-sensitive dextransucrase synthesis by a lactobacillus. J. Bacteriol. 86: 1079–1083.
L K, DUNICAN, H W, SEELEY
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Dextransucrase from Streptococcus sanguis Further Characterization
Caries Research, 1971Further 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 ...
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The dissociation of aggregate forms of dextransucrase
Archives of Biochemistry and Biophysics, 1982Abstract Aggregate forms of dextransucrase obtained from Streptococcus sanguis dissociate in the presence of sodium dodecyl sulfate. However, the enzyme was unstable under these conditions. Nonionic detergents such as Triton X-100 stabilize the enzyme (A. W. Miller and J. R. Robyt, (1981) Fed. Proc. Fed. Amer. Soc. Exp. Biol.
G A, Luzio, D A, Grahame, R M, Mayer
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Regulation of Dextransucrase Formation by Streptococcus sanguis
Caries Research, 1973The dextransucrase formation by Streptococcus sanguis, strain 804, was studied under standardized and reproducible conditions in continuous culture. At state growth in complex medium the enzyme activity was high at low dilution rates and decreased when the dilution rate increased. At steady-state growth in chemically defined medium, the enzyme activity
J, Carlsson, B, Elander
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