Structural analysis of rebaudioside A derivatives obtained by Lactobacillus reuteri 180 glucansucrase-catalyzed trans-α-glucosylation

Gerwig, G. J., Te Poele, E. M., Dijkhuizen, L. & Kamerling, J. P., 31-Jan-2017, In : Carbohydrate Research. 440-441, p. 51-62 12 p.

Research output: Contribution to journalArticleAcademicpeer-review

The wild-type Gtf180-ΔN glucansucrase enzyme from Lactobacillus reuteri 180 was found to catalyze the α-glucosylation of the steviol glycoside rebaudioside A, using sucrose as glucosyl donor in a transglucosylation process. Structural analysis of the formed products by MALDI-TOF mass spectrometry, methylation analysis and NMR spectroscopy showed that rebaudioside A is specifically α-d-glucosylated at the steviol C-19 β-d-glucosyl moiety (55% conversion). The main product is a mono-(α1 → 6)-glucosylated derivative (RebA-G1). A series of minor products, up to the incorporation of eight glucose residues, comprise elongations of RebA-G1 with mainly alternating (α1 → 3)- and (α1 → 6)-linked glucopyranose residues. These studies were carried out in the context of a program directed to the improvement of the taste of steviol glycosides via enzymatic modification of their naturally occurring carbohydrate moieties.

Original languageEnglish
Pages (from-to)51-62
Number of pages12
JournalCarbohydrate Research
Publication statusPublished - 31-Jan-2017


  • Stevia rebaudiana, sweetener, steviol glucosides, carbohydrate, NMR spectroscopy, glycobiotechnology

Download statistics

No data available

ID: 40011057