Kinetic properties of an inulosucrase from Lactobacillus reuteri 121
article
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
Topics
Food technologyFructosyltransferaseSucroseBacterial enzymeInulosucraseUnclassified drugCarboxy terminal sequenceCatalysisChemical analysisEnzyme activityEnzyme kineticsEnzyme purificationEnzyme substrateEnzyme synthesisEscherichia coliHill reactionLactobacillus reuteriMichaelis Menten kineticsNonhumanNucleotide sequenceHexosyltransferasesHydrogen-Ion ConcentrationHydrolysisKineticsLactobacillusMetalsRecombinant ProteinsSequence DeletionTemperatureBacteria (microorganisms)LactobacillusLactobacillus reu
TNO Identifier
42463
Source
FEBS Letters, 534, pp. 207-210.
Pages
207-210