Kinetic properties of an inulosucrase from Lactobacillus reuteri 121

FEBS Lett. 2003 Jan 16;534(1-3):207-10. doi: 10.1016/s0014-5793(02)03841-3.


Inulosucrases catalyze transfer of a fructose moiety from sucrose to a water molecule (hydrolysis) or to an acceptor molecule (transferase), yielding inulin. Bacterial inulin production is rare and a biochemical analysis of inulosucrase enzymes has not been reported. Here we report biochemical characteristics of a purified recombinant inulosucrase enzyme from Lactobacillus reuteri. It displayed Michaelis-Menten type of kinetics with substrate inhibition for the hydrolysis reaction. Kinetics of the transferase reaction is best described by the Hill equation, not reported before for these enzymes. A C-terminal deletion of 100 amino acids did not appear to affect enzyme activity or product formation. This truncated form of the enzyme was used for biochemical characterization.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Hexosyltransferases / drug effects
  • Hexosyltransferases / genetics
  • Hexosyltransferases / metabolism*
  • Hydrogen-Ion Concentration
  • Hydrolysis
  • Kinetics
  • Lactobacillus / enzymology*
  • Metals / metabolism
  • Metals / pharmacology
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Sequence Deletion
  • Temperature


  • Metals
  • Recombinant Proteins
  • Hexosyltransferases
  • inulosucrase