Kinetic properties of an inulosucrase from Lactobacillus reuteri 121

Kinetic properties of an inulosucrase from Lactobacillus reuteri 121

TNO Voeding Centraal Instituut voor Voedingsonderzoek TNO
van Hijum, S.A.F.T.
van der Maarel, M.J.E.C.
Dijkhuizen, L.

2003

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. © 2002 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved. Molecular Sequence Numbers: GENBANK: AF459437; Chemicals/CAS: Hexosyltransferases, EC 2.4.1.-; inulosucrase, EC 2.4.1.9; Metals; Recombinant Proteins

Food technology
Fructosyltransferase
Sucrose
Bacterial enzyme
Inulosucrase
Unclassified drug
Carboxy terminal sequence
Catalysis
Chemical analysis
Enzyme activity
Enzyme kinetics
Enzyme purification
Enzyme substrate
Enzyme synthesis
Escherichia coli
Hill reaction
Lactobacillus reuteri
Michaelis Menten kinetics
Nonhuman
Nucleotide sequence
Hexosyltransferases
Hydrogen-Ion Concentration
Hydrolysis
Kinetics
Lactobacillus
Metals
Recombinant Proteins
Sequence Deletion
Temperature
Bacteria (microorganisms)
Lactobacillus
Lactobacillus reu

http://resolver.tudelft.nl/uuid:22455fe3-ae26-40bb-9c4c-028921b8a147

https://doi.org/10.1016/s0014-5793(02)03841-3

42463

FEBS Letters, 534 (534), 207-210

article