Please use this identifier to cite or link to this item: doi:10.22028/D291-30939
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Title: Glucansucrase (mutant) enzymes from Lactobacillus reuteri 180 efficiently transglucosylate Stevia component rebaudioside A, resulting in a superior taste
Author(s): Te Poele, Evelien M.
Devlamynck, Tim
Jäger, Manuel
Gerwig, Gerrit J.
Van de Walle, Davy
Dewettinck, Koen
Hirsch, Anna
Kamerling, Johannis P.
Soetaert, Wim
Dijkhuizen, Lubbert
Language: English
Title: Scientific reports
Volume: 8
Issue: 1
Publisher/Platform: Springer
Year of Publication: 2018
Publikation type: Journal Article
Abstract: Steviol glycosides from the leaves of the plant Stevia rebaudiana are high-potency natural sweeteners but suffer from a lingering bitterness. The Lactobacillus reuteri 180 wild-type glucansucrase Gtf180-ΔN, and in particular its Q1140E-mutant, efficiently α-glucosylated rebaudioside A (RebA), using sucrose as donor substrate. Structural analysis of the products by MALDI-TOF mass spectrometry, methylation analysis and NMR spectroscopy showed that both enzymes exclusively glucosylate the Glc(β1→C-19 residue of RebA, with the initial formation of an (α1→6) linkage. Docking of RebA in the active site of the enzyme revealed that only the steviol C-19 β-D-glucosyl moiety is available for glucosylation. Response surface methodology was applied to optimize the Gtf180-ΔN-Q1140E-catalyzed α-glucosylation of RebA, resulting in a highly productive process with a RebA conversion of 95% and a production of 115 g/L α-glucosylated products within 3 h. Development of a fed-batch reaction allowed further suppression of α-glucan synthesis which improved the product yield to 270 g/L. Sensory analysis by a trained panel revealed that glucosylated RebA products show a significant reduction in bitterness, resulting in a superior taste profile compared to RebA. The Gtf180-ΔN-Q1140E glucansucrase mutant enzyme thus is an efficient biocatalyst for generating α-glucosylated RebA variants with improved edulcorant/organoleptic properties.
DOI of the first publication: 10.1038/s41598-018-19622-5
URL of the first publication: https://www.nature.com/articles/s41598-018-19622-5
Link to this record: hdl:20.500.11880/29152
http://dx.doi.org/10.22028/D291-30939
ISSN: 2045-2322
Date of registration: 14-May-2020
Faculty: NT - Naturwissenschaftlich- Technische Fakultät
Department: NT - Pharmazie
Professorship: NT - Prof. Dr. Anna Hirsch
Collections:UniBib – Die Universitätsbibliographie

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