Abstract
Publisher Summary This chapter discusses the kinetics and reaction engineering of oligosaccharide synthesis with dextransucrase. Experiments are performed with free and immobilized enzyme with no significant difference in the reaction kinetics; high efficiencies of immobilized dextransucrase were obtained. The kinetic investigations allow giving a quantitative estimate for the acceptor strength based on the kinetic parameters of the acceptor reaction. In the study, it is found that acceptors will compete with the substrate for the acceptor-binding site. Strong acceptors such as maltose accelerate the overall reaction rate, up to a factor of over two, because of a faster acceptor reaction than dextran formation rate. Further, in the presence of the weak fructose acceptor, the slow acceptor reaction becomes the dominating step at high fructose concentrations resulting in a decrease of the overall reaction rate; maximal rates of leucrose formation were 20% of the reaction rate without acceptor.
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