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Kinetic properties of an inulosucrase from Lactobacillus reuteri 121
Author(s) -
van Hijum S.A.F.T,
van der Maarel M.J.E.C,
Dijkhuizen L
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03841-3
Subject(s) - lactobacillus reuteri , chemistry , inulin , enzyme , enzyme kinetics , product inhibition , hydrolysis , substrate (aquarium) , biochemistry , transferase , moiety , fructose , lactobacillus acidophilus , kinetics , michaelis–menten kinetics , enzyme assay , stereochemistry , lactobacillus , bacteria , active site , non competitive inhibition , fermentation , biology , probiotic , ecology , physics , quantum mechanics , genetics
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.