Please use this identifier to cite or link to this item:Volltext verfügbar? / Dokumentlieferung
|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.|
Gerwig, Gerrit J.
Van de Walle, Davy
Kamerling, Johannis P.
|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|
|Date of registration:||14-May-2020|
|Faculty:||NT - Naturwissenschaftlich- Technische Fakultät|
|Department:||NT - Pharmazie|
|Professorship:||NT - Prof. Dr. Anna Hirsch|
|Collections:||UniBib – Die Universitätsbibliographie|
Files for this record:
There are no files associated with this item.
Items in SciDok are protected by copyright, with all rights reserved, unless otherwise indicated.