Acceptor-induced modification of regioselectivity in CGTase-catalyzed glycosylations of p-nitrophenyl-glucopyranosides

Strompen, Simon; Miranda-Molina, Alfonso; López-Munguı́a, Agustı́n; Castillo, Edmundo; Saab‐Rincón, Gloria

doi:10.1016/j.carres.2014.11.010

Cited by 9 publications

(12 citation statements)

References 40 publications

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“…Then, we studied the effect of temperature on the reaction course. Figure 5 represents the formation of hesperetin monoglucoside at different temperatures (50–80 °C) after 18 h. As illustrated, 60 °C was the optimum temperature, in accordance with other biotransformations catalyzed by this enzyme [ 39 , 46 ], since this temperature represents a compromise between enzyme activity and protein stability.…”

Section: Resultssupporting

confidence: 68%

Optimization of Regioselective α-Glucosylation of Hesperetin Catalyzed by Cyclodextrin Glucanotransferase

et al. 2018

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The regioselective α-glucosylation of hesperetin was achieved by a transglycosylation reaction catalyzed by cyclodextrin glucanotransferase (CGTase) from Thermoanaerobacter sp. using soluble starch as glucosyl donor. By combining mass spectrometry (ESI-TOF) and 2D-NMR analysis, the main monoglucosylated derivative was fully characterized (hesperetin 7-O-α-d-glucopyranoside). In order to increase the yield of monoglucoside, several reaction parameters were optimized: Nature and percentage of cosolvent, composition of the aqueous phase, glucosyl donor, temperature, and the concentrations of hesperetin and soluble starch. Under the optimal conditions, which included the presence of 30% of bis(2-methoxyethyl) ether as cosolvent, the maximum concentration of monoglucoside was approximately 2 mM, obtained after 24 h of reaction. To our knowledge, this is the first report of direct glucosylation of hesperetin employing free enzymes instead of whole cells.

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Section: Resultssupporting

confidence: 68%

Optimization of Regioselective α-Glucosylation of Hesperetin Catalyzed by Cyclodextrin Glucanotransferase

et al. 2018

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“…, organic, inorganic, or biological molecules) to increase their solubility, stability, and bioavailability 2 . Since functional characterizations of CDs have been primarily addressed for biotechnological and pharmaceutical applications 3 – 5 , their physiological purpose has not been thoroughly discussed. Nevertheless, the role of CDs seems to be related to resource competition in microbial communities, such as monopolizing substrate availability or mitigating the toxicity of surrounding organic substrates and volatiles 6 , 7 , as well as carrying antimicrobial and signaling molecules 8 , 9 .…”

Section: Introductionmentioning

confidence: 99%

Mining for novel cyclomaltodextrin glucanotransferases unravels the carbohydrate metabolism pathway via cyclodextrins in Thermoanaerobacterales

Centeno-Leija

Espinosa-Barrera

Velazquez-Cruz

et al. 2022

Sci Rep

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Carbohydrate metabolism via cyclodextrins (CM-CD) is an uncommon starch-converting pathway that thoroughly depends on extracellular cyclomaltodextrin glucanotransferases (CGTases) to transform the surrounding starch substrate to α-(1,4)-linked oligosaccharides and cyclodextrins (CDs). The CM-CD pathway has emerged as a convenient microbial adaptation to thrive under extreme temperatures, as CDs are functional amphipathic toroids with higher heat-resistant values than linear dextrins. Nevertheless, although the CM-CD pathway has been described in a few mesophilic bacteria and archaea, it remains obscure in extremely thermophilic prokaryotes (Topt ≥ 70 °C). Here, a new monophyletic group of CGTases with an exceptional three-domain ABC architecture was detected by (meta)genome mining of extremely thermophilic Thermoanaerobacterales living in a wide variety of hot starch-poor environments on Earth. Functional studies of a representative member, CldA, showed a maximum activity in a thermoacidophilic range (pH 4.0 and 80 °C) with remarkable product diversification that yielded a mixture of α:β:γ-CDs (34:62:4) from soluble starch, as well as G3–G7 linear dextrins and fermentable sugars as the primary products. Together, comparative genomics and predictive functional analysis, combined with data of the functionally characterized key proteins of the gene clusters encoding CGTases, revealed the CM-CD pathway in Thermoanaerobacterales and showed that it is involved in the synthesis, transportation, degradation, and metabolic assimilation of CDs.

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“…1.19), belongs to glycoside hydrolase (GH) family 13, a group of α-amylase enzymes that contains α-amylases, isoamylases, amylopullulanases, pullulanases, neopullulanases, and branching enzymes. 4 CGTase is mainly expressed in Bacillus sp. and employed to transglycosylate glucosyl residues to sugars, glycosides, and nonsugar compounds such as sugar alcohols, polyols, polyphenols, flavonoids, saponins, and vitamins.…”

Section: ■ Introductionmentioning

confidence: 99%

“…4,5 CGTase has been reported to primarily transglycosylate donor molecules to α(1→4)-glycosidic linkages and to α(1→6)-glycosidic linkages. 4 Enzymatic transglycosylation has been employed to modify the physiochemical properties of various compounds in foods such as elongation of 13-Oglucosyl to improve the sweetness of stevioside. 6,7 Mono-or disaccharides are also transferred by the enzyme to acceptor molecules such as ascorbic acid to form either α(1→3)-, α(1→ 4), or α(1→6)-glycosidic linkages.…”

Section: ■ Introductionmentioning

confidence: 99%

“…Glucanotransferases are enzymes that transfer glucosyl moieties derived from sucrose, cyclodextrins, or starches to synthesize dextrans or glucans . In particular, one of the glucanotransferases, cyclodextrin glucanotransferase (CGTase; EC 2.4.1.19), belongs to glycoside hydrolase (GH) family 13, a group of α-amylase enzymes that contains α-amylases, isoamylases, amylopullulanases, pullulanases, neopullulanases, and branching enzymes . CGTase is mainly expressed in Bacillus sp.…”

Section: Introductionmentioning

confidence: 99%

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Enzymatic Synthesis of a Novel Kaempferol-3-O-β-d-glucopyranosyl-(1→4)-O-α-d-glucopyranoside Using Cyclodextrin Glucanotransferase and Its Inhibitory Effects on Aldose Reductase, Inflammation, and Oxidative Stress

Choung

Hwang

et al. 2017

J. Agric. Food Chem.

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Kaempferol-3-O-β-d-glucopyranoside (astragalin, AS), a major flavonoid that exists in various plants, exerts antioxidant, antitumor, anti-human immunodeficiency virus (HIV), and anti-inflammatory effects. However, the low water solubility of AS limits its use. In this study, we used cyclodextrin glucanotransferase (CGTase) with maltose (G2) as a donor molecule to enzymatically modify AS to improve its water solubility and physiochemical properties. We isolated the glycosylated astragalin (G1-AS) and identified the structure of G1-AS as kaempferol-3-O-β-d-glucopyranosyl-(1→4)-O-α-d-glucopyranoside, where one glucose residue was transferred to AS. G1-AS retained the antioxidative activity of the original AS compound; however, the solubility of G1-AS was 65-fold higher than that of AS. In addition, G1-AS showed enhanced anti-inflammatory effects and aldose reductase inhibitory activity compared to AS when applied to rat lenses.

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Acceptor-induced modification of regioselectivity in CGTase-catalyzed glycosylations of p-nitrophenyl-glucopyranosides

Cited by 9 publications

References 40 publications

Optimization of Regioselective α-Glucosylation of Hesperetin Catalyzed by Cyclodextrin Glucanotransferase

Optimization of Regioselective α-Glucosylation of Hesperetin Catalyzed by Cyclodextrin Glucanotransferase

Mining for novel cyclomaltodextrin glucanotransferases unravels the carbohydrate metabolism pathway via cyclodextrins in Thermoanaerobacterales

Enzymatic Synthesis of a Novel Kaempferol-3-O-β-d-glucopyranosyl-(1→4)-O-α-d-glucopyranoside Using Cyclodextrin Glucanotransferase and Its Inhibitory Effects on Aldose Reductase, Inflammation, and Oxidative Stress

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