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Kinetic properties of an inulosucrase from Lactobacillus reuteri 121

Author: Hijum, S.A.F.T. van · Maarel, M.J.E.C. van der · Dijkhuizen, L.
Type:article
Date:2003
Institution: TNO Voeding Centraal Instituut voor Voedingsonderzoek TNO
Source:FEBS Letters, 534, 207-210
Identifier: 42463
doi: doi:10.1016/S0014-5793(02)03841-3
Keywords: 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

Abstract

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