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Consistent with electrostatic binding were the pI of the enzyme, the rate of synthesis being dependent on the degree of dextran carboxymethylation, and the greater inhibition of the enzyme by NaCl on a surface compared with that in solution see Supporting Information
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Consistent with electrostatic binding were the pI of the enzyme, the rate of synthesis being dependent on the degree of dextran carboxymethylation, and the greater inhibition of the enzyme by NaCl on a surface compared with that in solution (see Supporting Information).
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Amylosucrase forms an insoluble α-1,4 linked glucan from sucrose Rolland-Sabaté, A, Colonna, P, Potocki-Véronèse, G, Monsan, P, Planchot, V. J. Cereal Sci. 2004, 40, 17-30, We have shown that α-1,6 dextrans are not acceptors with this enzyme and surface extension cannot be detected despite enzyme binding to the surface. Therefore, substrate specificity was maintained on the surface and noncovalent interactions between glucan produced in bulk solution and the surface did not occur
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Amylosucrase forms an insoluble α-1,4 linked glucan from sucrose (Rolland-Sabaté, A.; Colonna, P.; Potocki-Véronèse, G.; Monsan, P.; Planchot, V. J. Cereal Sci. 2004, 40, 17-30). We have shown that α-1,6 dextrans are not acceptors with this enzyme and surface extension cannot be detected despite enzyme binding to the surface. Therefore, substrate specificity was maintained on the surface and noncovalent interactions between glucan produced in bulk solution and the surface did not occur.
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