| Literature DB >> 12527388 |
S A F T van Hijum1, M J E C van der Maarel, L Dijkhuizen.
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.Entities:
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Year: 2003 PMID: 12527388 DOI: 10.1016/s0014-5793(02)03841-3
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124