Trans-α-glucosylation of stevioside by the mutant glucansucrase enzyme Gtf180-ΔN-Q1140E improves its taste profile

Devlamynck, Tim; Poele, Evelien M. te; Quataert, Koen; Gerwig, Gerrit J.; Walle, Davy Van de; Dewettinck, Koen; Kamerling, Johannis P.; Soetaert, Wim; Dijkhuizen, Lubbert

doi:10.1016/j.foodchem.2018.08.025

Cited by 31 publications

(16 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…On the other hand, glucansucrases are more promising enzymes in the modification of steviol glycosides, since they form a-1,6 and 1,3-glycosidic bonds, which are not hydrolyzed by human enzymes. Moreover, they can use low-cost donors, such as sucrose, reaching product yields over 90% (Ko et al, 2016;Devlamynck et al, 2019;Son et al, 2020). Regarding plantderived UDP-glucosyltransferase-mediated bioconversion, the regeneration of UDP sugar donors with sucrose synthase is necessary, but yields over 70% can be obtained (Wang et al, 2016;Chen et al, 2021Chen et al, , 2020Chen et al, , 2018.…”

Section: Discussionmentioning

confidence: 99%

β-Glucosidase and β-Galactosidase-Mediated Transglycosylation of Steviol Glycosides Utilizing Industrial Byproducts

Zerva

Chorozian

Kritikou

et al. 2021

Front. Bioeng. Biotechnol.

View full text Add to dashboard Cite

Stevia rebaudiana Bertoni is a plant cultivated worldwide due to its use as a sweetener. The sweet taste of stevia is attributed to its numerous steviol glycosides, however, their use is still limited, due to their bitter aftertaste. The transglycosylation of steviol glycosides, aiming at the improvement of their taste, has been reported for many enzymes, however, glycosyl hydrolases are not extensively studied in this respect. In the present study, a β-glucosidase, MtBgl3a, and a β-galactosidase, TtbGal1, have been applied in the transglycosylation of two steviol glycosides, stevioside and rebaudioside A. The maximum conversion yields were 34.6 and 33.1% for stevioside, while 25.6 and 37.6% were obtained for rebaudioside A conversion by MtBgl3a and TtbGal1, respectively. Low-cost industrial byproducts were employed as sugar donors, such as cellulose hydrolyzate and acid whey for TtbGal1- and MtBgl3a- mediated bioconversion, respectively. LC-HRMS analysis identified the formation of mono- and di- glycosylated products from stevioside and rebaudioside A. Overall, the results of the present work indicate that both biocatalysts can be exploited for the design of a cost-effective process for the modification of steviol glycosides.

show abstract

Section: Discussionmentioning

confidence: 99%

β-Glucosidase and β-Galactosidase-Mediated Transglycosylation of Steviol Glycosides Utilizing Industrial Byproducts

Zerva

Chorozian

Kritikou

et al. 2021

Front. Bioeng. Biotechnol.

View full text Add to dashboard Cite

show abstract

“…The product is approved and introduced to some markets as “Glucosylated Stevia Leaf Extract”. CarbExplore utilizes a glucansucrase to glucosylate on the C19‐sugar—here the new bond is α‐1,6 [162] . This synthesis is highly efficient, reaching 270 g L −1 in 3 h with 94 % conversion [163] .…”

Section: Glycosylationmentioning

confidence: 99%

“…CarbExplore utilizes aglucansucrase to glucosylate on the C19-sugar-here the new bond is a-1,6. [162] This synthesis is highly efficient, reaching 270 gL À1 in 3h with 94 %c onversion. [163] However,t he a-glucosidic products are not truly natural.…”

Section: Stevia Glucosides/ Rebaudiosidesmentioning

confidence: 99%

Biocatalysis: Enzymatic Synthesis for Industrial Applications

et al. 2020

View full text Add to dashboard Cite

in 2007, followed by postdoctoral studies at York University (UK) and Greifswald University (Germany). In 2010, she transitionedto industry applying and developing biocatalytic technologies at Novacta in the UK, prior to joining Chemical Process Development at GSK, with responsibility for the development and implementation of new biocatalytic technologyi nboth pre-and post-commercialization routes. Since Dec. 2016, Radka is leading the Bioreactions group in GDC at the Novartis Institute for Biomedical Research in Basel, Switzerland. Jeffrey Moore obtained his PhD in Chemical Engineeringf rom the California Institute of Technology in 1996 as Frances Arnold's first Directed Evolution graduate student. His foundational work led to an evolved p-nitrobenzyl esterase and the Lonza Centenary Prize (1997). In 1996, he joined the Biocatalysis Group of Merck & Co.in Rahway NJ, spending two decades inventing new enzymes and new enzymatic processes. In 2018, he transitionedtothe Merck Protein EngineeringG roup responsible for evolving enzymes for the discovery,d evelopmenta nd commercials cale manufacture of medicines. He has been awarded aUS Presidential Green Chemistry Award (2010), the BioCat2012 Award (2012) and the Thomas Edison Inventorship Award (2014). Kai Baldenius studied chemistry in Hamburg and Southampton. He received his PhD for research in asymmetric organometallic catalysis, supervised by H. tom Dieck and H. B. Kagan. After his postdoc on natural product synthesis with K. C. Nicolaou at the Scripps Research Institute he joined BASF in 1993. Kai served BASF in various functions (R&D, production, marketing, sales) before he took the lead of BASF'sbiocatalysis research for almost ad efcade. He left BASF to become afree-lancing consultanti n2019 and in 2020 he has founded Baldenius Biotech Consulting. Uwe T. Bornscheuer studied chemistry and received his PhD in 1993 at Hannover University followed by apostdoc at Nagoya University (Japan). In 1998, he completed his Habilitation at Stuttgart University about the use of lipases and esterasesi n organic synthesis. He has been Professor at the Institute of Biochemistry at Greifswald University since 1999. Beside other awards, he received in 2008 the BioCat2008 Award. He was just recognized as "Chemistry Europe Fellow". His current research interest focuses on the discovery and engineering of enzymes from various classes for applications in organic synthesis, lipid modification, degradation of plastics or complex marine polysaccharides.

show abstract

“…CarbExplore nutzt eine Glucansucrase,umden C19-Zucker aufzuglukosylieren -d abei wird die neue anomere Bindung a-1,6 gebildet. [162] Diese Synthese ist hocheffizient und erreicht 270 gL À1 in 3hmit 94 %Umsatz ausgehend von Reb A 99 b. [163] Allerdings sind die erhaltenen a-glukosidischen Stevia-Derivate nicht wirklich natürlich.…”

Section: Methodsunclassified

“…Das Produkt ist in einigen Märkten zugelassen und als “Glucosylated Stevia Leaf Extract ” eingeführt. CarbExplore nutzt eine Glucansucrase, um den C19‐Zucker aufzuglukosylieren – dabei wird die neue anomere Bindung α‐1,6 gebildet [162] . Diese Synthese ist hocheffizient und erreicht 270 g L −1 in 3 h mit 94 % Umsatz ausgehend von Reb A 99 b [163] .…”

Section: Glykosylierungenunclassified

Biokatalyse: Enzymatische Synthese für industrielle Anwendungen

et al. 2020

View full text Add to dashboard Cite

www.angewandte.de 2020 Die Autoren. Verçffentlicht von Wiley-VCH GmbH. Dieser Open Access Beitrag steht unter den Bedingungend er Creative Commons AttributionN on-CommercialN oDerivs License, die eine Nutzung und Verbreitung in allen Medien gestattet, sofern der ursprüngliche Beitrag ordnungsgemäßzitiert und nicht fürkommerzielle Zwecke genutzt wird und keine ¾nderungen und Anpassungen vorgenommen werden.

show abstract

Trans-α-glucosylation of stevioside by the mutant glucansucrase enzyme Gtf180-ΔN-Q1140E improves its taste profile

Cited by 31 publications

References 27 publications

β-Glucosidase and β-Galactosidase-Mediated Transglycosylation of Steviol Glycosides Utilizing Industrial Byproducts

β-Glucosidase and β-Galactosidase-Mediated Transglycosylation of Steviol Glycosides Utilizing Industrial Byproducts

Biocatalysis: Enzymatic Synthesis for Industrial Applications

Biokatalyse: Enzymatische Synthese für industrielle Anwendungen

Contact Info

Product

Resources

About