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doi:10.22028/D291-30939
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: | SpringerNature |
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: | SciDok - Der Wissenschaftsserver der Universität des Saarlandes |
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