title: Kinetic studies of dextransucrase enzyme reactions on a substrate- or enzyme-immobilized 27 MHz quartz crystal microbalance.
abstract: Catalytic elongation by dextransucrase (DSase) was monitored directly on a dextran-acceptor- or DSase-immobilized 27 MHz quartz crystal microbalance (QCM). Kinetic parameters for the binding of the enzyme to the dextran acceptor (k(on), k(off), and K(d)) and enzymatic elongation in the presence of a sucrose monomer (K(m) for sucrose and k(cat)) were determined. The kinetic parameters obtained by both methods were consistent.
authors.affiliation: Department of Biomolecular Engineering, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama, 226-8501 Japan.
authors.forename: Takanori
authors.initials: T
authors.lastname: Nihira
authors.forename: Toshiaki
authors.initials: T
authors.lastname: Mori
authors.forename: Megumi
authors.initials: M
authors.lastname: Asakura
authors.forename: Yoshio
authors.initials: Y
authors.lastname: Okahata
mesh_terms: D003911:Dextrans / Q000737:chemistry / Q000378:metabolism; D004789:Enzyme Activation; D004800:Enzymes, Immobilized / Q000737:chemistry / Q000378:metabolism*; D005964:Glucosyltransferases / Q000737:chemistry / Q000378:metabolism*; D007700:Kinetics; D058525:Quartz Crystal Microbalance Techniques; D013379:Substrate Specificity
chemical_list: D003911:Dextrans; D004800:Enzymes, Immobilized; D005964:Glucosyltransferases; C020025:dextransucrase