Recent Developments in Preparative Enzymatic Syntheses of Carbohydrates

Rowan, Andrew S.; Hamilton, Chris J.

doi:10.1002/chin.200637245

Cited by 3 publications

(5 citation statements)

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“…Thus, transglycosylation reactions are widely employed to modify phenolic compounds such as hydroquinone, resveratrol, genistein and catechin to produce their respective glucosides [21][22][23][24]. There are several reports of transglycosylation reactions and comparative study of their biological activities with aglycones [25][26][27][28]. However, in some instances, the trace amount of substrate remained in the sample could be harmful.…”

Section: Discussionmentioning

confidence: 99%

Sustainable Production of Dihydroxybenzene Glucosides Using Immobilized Amylosucrase from Deinococcus geothermalis

Lee¹,

Kim²,

Parajuli³

et al. 2018

Journal of Microbiology and Biotechnology

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The amylosucrase encoding gene from Deinococcus geothermalis DSM 11300 (DgAS) was codonoptimized and expressed in Escherichia coli. The enzyme was employed for biosynthesis of three different dihydroxybenzene glucosides using sucrose as the source of glucose moiety. The reaction parameters, including temperature, pH, and donor (sucrose) and acceptor substrate concentrations, were optimized to increase the production yield. This study demonstrates the highest ever reported molar yield of hydroquinone glucosides 325.6 mM (88.6 g/l), resorcinol glucosides 130.2 mM (35.4 g/l) and catechol glucosides 284.4 mM (77.4 g/l) when 400 mM hydroquinone, 200 mM resorcinol and 300 mM catechol, respectively, were used as an acceptor substrate. Furthermore, the use of commercially available amyloglucosidase at the end of the transglycosylation reaction minimized the glucooligosaccharides, thereby enhancing the target productivity of mono-glucosides. Moreover, the immobilized DgAS on Amicogen LKZ118 beads led to a 278.4 mM (75.8 g/l), 108.8 mM (29.6 g/l) and 211.2 mM (57.5 g/l) final concentration of mono-glycosylated product of hydroquinone, catechol and resorcinol at 35 cycles, respectively, when the same substrate concentration was used as mentioned above. The percent yield of the total glycosides of hydroquinone and catechol varied from 85% to 90% during 35 cycles of reactions in an immobilized system, however, in case of resorcinol the yield was in between 65% to 70%. The immobilized DgAS enhanced the efficiency of the glycosylation reaction and is therefore considered effective for industrial application.

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Section: Discussionmentioning

confidence: 99%

Sustainable Production of Dihydroxybenzene Glucosides Using Immobilized Amylosucrase from Deinococcus geothermalis

Lee¹,

Kim²,

Parajuli³

et al. 2018

Journal of Microbiology and Biotechnology

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“…Consequently, the DHAP-dependent aldolases offer the opportunity to carry out in a controlled fashion different stereochemically complementary carbon-carbon bond aldol reactions. This has been widely exploited on laboratory scale over the past two decades (Fessner and Walter 1996;Fessner 1998;Silvestri et al 2003;Rowan and Hamilton 2006), in particular, in the area of iminocyclitols, which can inhibit glycosidases and are, therefore, studied for antiviral, anticancer, antidiabetic, and pesticidal properties (Whalen and Wong 2006).…”

Section: Introductionmentioning

confidence: 99%

Chemical and enzymatic routes to dihydroxyacetone phosphate

Schümperli

Pellaux

Panke

2007

Appl Microbiol Biotechnol

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Stereoselective carbon-carbon bond formation with aldolases has become an indispensable tool in preparative synthetic chemistry. In particular, the dihydroxyacetone phosphate (DHAP)-dependent aldolases are attractive because four different types are available that allow access to a complete set of diastereomers of vicinal diols from achiral aldehyde acceptors and the DHAP donor substrate. While the substrate specificity for the acceptor is rather relaxed, these enzymes show only very limited tolerance for substituting the donor. Therefore, access to DHAP is instrumental for the preparative exploitation of these enzymes, and several routes for its synthesis have become available. DHAP is unstable, so chemical synthetic routes have concentrated on producing a storable precursor that can easily be converted to DHAP immediately before its use. Enzymatic routes have concentrated on integrating the DHAP formation with upstream or downstream catalytic steps, leading to multi-enzyme arrangements with up to seven enzymes operating simultaneously. While the various chemical routes suffer from either low yields, complicated work-up, or toxic reagents or catalysts, the enzymatic routes suffer from complex product mixtures and the need to assemble multiple enzymes into one reaction scheme. Both types of routes will require further improvement to serve as a basis for a scalable route to DHAP.

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“…The most abundant class of enzymes forming glycosidic bonds in nature, they are usually highly regioselective and enantioselective and have been widely applied in organic synthesis. 47,48 Many of these enzymes are membrane associated, like the mammalian UDP-glucurosyltransferases, but there are also many soluble enzymes, such as the UDP-glucosyltransferases that serve to solubilize xenobiotics in plants by forming their glucosides. Plants appear to be particularly rich sources of glycosyltransferases: less than 30 such enzymes have been identified in the human genome, 49 yet there are 117 putative glycosyltransferases in the genome of Arabidopsis thaliana, a species used as a model system by molecular biologists due to the small size of its genome relative to that of other plants.…”

Section: Phase II Metabolic Transformationsmentioning

confidence: 99%

“…52 Glycosynthases are now available for the formation of a diverse range of b-(1!3)-, b-(1!4)-, b-(1!6)-and -(1!4)-linked oligosaccharides. 48 The increasing availability of biocatalytic tools for glycosylation is applicable to the drug discovery process as well as to metabolite preparation and synthesis of established glycosidic active ingredients. There is growing interest in the discovery of new polysaccharide-containing drugs.…”

Section: Phase II Metabolic Transformationsmentioning

confidence: 99%

“…Glycorandomization, a powerful biocatalytic approach to the generation of libraries of unnatural polysaccharides through the use of enzyme variants with relaxed substrate specificity, represents one important approach towards this end. 48 In summary, biocatalysis offers a number of alternatives to chemical synthesis for the selective preparation of metabolites. The use of recombinant human CYPs is an attractive method, as little screening is required and the enzymes catalyse a broad range of metabolic reactions.…”

Section: Phase II Metabolic Transformationsmentioning

confidence: 99%

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