β-Galactosidase transferase activity in ice and use of vinyl-β-d-galactoside as donor

Chiffoleau-Giraud, Violaine; Spangenberg, Petra; Rabiller, Claude

doi:10.1016/s0957-4166(97)00194-8

Cited by 23 publications

(8 citation statements)

References 17 publications

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“…As this is often not the case, an excess of the activated sugar donor is required under kinetic control. Similar to the coupling of protected glycosyl donors, the donors for transglycosylation, such as fluoro [59,60,61,62], -azido [63], p -nitrophenyl- [64] or p -nitropyridyl- [65], vinyl- [66], and allyl-glycosides [67] require their separate synthesis. The direct glycosylation is challenging due to the poor K eq under aqueous reaction conditions, limiting the degree of conversion.…”

Section: Glycosyltransferases In Naturementioning

confidence: 99%

Leloir Glycosyltransferases in Applied Biocatalysis: A Multidisciplinary Approach

Mestrom

Przypis

Kowalczykiewicz

et al. 2019

IJMS

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Enzymes are nature's catalyst of choice for the highly selective and efficient coupling of carbohydrates. Enzymatic sugar coupling is a competitive technology for industrial glycosylation reactions, since chemical synthetic routes require extensive use of laborious protection group manipulations and often lack regio-and stereoselectivity. The application of Leloir glycosyltransferases has received considerable attention in recent years and offers excellent control over the reactivity and selectivity of glycosylation reactions with unprotected carbohydrates, paving the way for previously inaccessible synthetic routes. The development of nucleotide recycling cascades has allowed for the efficient production and reuse of nucleotide sugar donors in robust one-pot multi-enzyme glycosylation cascades. In this way, large glycans and glycoconjugates with complex stereochemistry can be constructed. With recent advances, LeLoir glycosyltransferases are close to being applied industrially in multi-enzyme, programmable cascade glycosylations.hydroxynitrile lyases catalyzed the enzymatic hydrolysis of the glycoside amygdalin [3]. Moving almost two centuries forward, the largest volumetric biocatalytic industrial process is the application of glucose isomerase for the production of high fructose syrup for food and drink applications, producing fructose from glucose at 10 7 tons per year [4]. The secret of the success of enzymes in the production or treatment of carbohydrates and glycosides is their exquisite stereo-and regioselectivity. The excellent selectivity of enzymes is required due to the diversity of structural features of carbohydrates [5], comprising d-and l-epimers, ring size, anomeric configuration, linkages, branching, and oxidation state(s). Since drug targets often exhibit specificity for all of these structural features, the production process should not contain any side-products to prevent undesired side-effects [6].The challenge in the synthesis of carbohydrates is their wide variety of functionalities and stereochemistry ( Figure 1). (Poly)hydroxyaldehydes containing a terminal aldehyde are referred to as aldoses and (poly)hydroxyketones are defined as ketoses. In aqueous solutions, monosaccharides form equilibrium mixtures of linear open-chain and ring-closed 5-or 6-membered furanoses or pyranoses, respectively. For aldoses, the asymmetric ring forms at C-1. For ketoses, it closes at C-2 as an axial (α) or equatorial (β) hemiacetal or hemiketal, respectively (commonly defined as the anomeric center). A glycosidic linkage is a covalent O-, S-, N-, or C-bond connecting a monosaccharide to another residue resulting in a glycoside, while glucoside is specific for a glucose moiety. The equatorial or axial position of the glycosidic bond is referred to as α-(axial) or β-linkage (equatorial). The number of carbohydrates linked via glycosidic bonds can be subdivided into oligosaccharides with two to ten linked carbohydrates, while polysaccharides (glycans) contain more than ten glycosidic bonds. A glycan either con...

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Section: Glycosyltransferases In Naturementioning

confidence: 99%

Leloir Glycosyltransferases in Applied Biocatalysis: A Multidisciplinary Approach

Mestrom

Przypis

Kowalczykiewicz

et al. 2019

IJMS

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“…To overcome this limitation, several protein engineering strategies, based on site directed mutagenesis (Mackensie et al 1998) or molecular directed evolution (Feng et al 2005), have been proposed to reduce and even eliminate the hydrolytic activities of glycosidases while keeping the transglycosylation activities. Other alternatives suggested to prevent the undesirable hydrolysis reaction were reducing the water activity by using organic solvents (van Rantwijk et al 1999) or using frozen buffer (ChiffoleauGiraud et al 1997). However, most of the water-immiscible solvents do not dissolve carbohydrate substrates while water-miscible solvents, such as DMSO and DMF, although dissolving carbohydrates, generally inactivate glycosidases at concentrations above 20%.…”

Section: Introductionmentioning

confidence: 99%

Correlation between thermostability and stability of glycosidases in ionic liquid

et al. 2011

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“…In order to improve the product yield, activated saccharides can be used as the glycosyl donors rather than native saccharides. Activated saccharides usually contain aryl or vinyl groups which are much better leaving groups in transglycosylation reaction than glycosyl units of natural sugars (Chiffoleau-Giraud, Spangenberg, & Rabiller, 1997;van Woudenberg-, Van Belle, Van Rantwijk, & Sheldon, 1998). For instance, Santin et al reported p-nitrophenyl β-D-galactopyranoside as the substrate of β-galactosidase from Sulfolobus solfataricus with an isolated glycomonomer yield of about 75% (Santin et al, 1996).…”

Section: Kinetically Controlled Transglycosylationmentioning

confidence: 99%

Synthesis of glycomonomers via biocatalytic methods

Adharis

Loos

2019

Methods in Enzymology

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β-Galactosidase transferase activity in ice and use of vinyl-β-d-galactoside as donor

Cited by 23 publications

References 17 publications

Leloir Glycosyltransferases in Applied Biocatalysis: A Multidisciplinary Approach

Leloir Glycosyltransferases in Applied Biocatalysis: A Multidisciplinary Approach

Correlation between thermostability and stability of glycosidases in ionic liquid

Synthesis of glycomonomers via biocatalytic methods

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