Efficient α-Glucosylation of Epigallocatechin Gallate Catalyzed by Cyclodextrin Glucanotransferase from <i>Thermoanaerobacter</i> Species

Gonzalez, Jose L. Ugia; Leemans, Laura; Poveda, Ana; Jiménez‐Barbero, Jesús; Ballesteros, Antonio; Plou, Francisco J.

doi:10.1021/acs.jafc.8b02143

Cited by 22 publications

(22 citation statements)

References 59 publications

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“…(Toruzyme 3.0L) [ 30 , 33 ], employing partially hydrolyzed starch (maltodextrins with DP ≤ 60) as glucosyl donor. This enzyme has demonstrated an extraordinary ability to glucosylate other mono- and polyphenolic compounds [ 26 , 31 , 32 , 34 , 35 , 36 , 37 , 38 ].…”

Section: Resultsmentioning

confidence: 99%

“…For glycosylation of flavonoids, the use of enzymes is a very attractive strategy due to their unique specificity and the mild conditions required for such biotransformations [ 23 , 24 , 25 , 26 , 27 ]. The enzymatic glycosylation of hesperetin has been scarcely investigated, and only a few reports have been published employing cultured cells from yeasts or plants.…”

Section: Introductionmentioning

confidence: 99%

“…In this work, we describe the enzymatic synthesis of an α-glucosylated derivative of hesperetin by a transglycosylation reaction catalyzed by a transglycosidase, namely cyclodextrin glycosyltransferase (CGTase, EC 2.4.1.19), which employs a renewable and easily available carbohydrate (starch) as glucosyl donor [ 30 ]. In previous works, we successfully achieved the α-glucosylation of a flavonoid (epigallocatechin gallate [ 26 ]) and two stilbenes (resveratrol [ 31 ], pterostilbene [ 32 ]) with this enzyme.…”

Section: Introductionmentioning

confidence: 99%

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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: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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

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“…In order to increase its stability and bioavailability (35), and to reduce its astringency for food applications (36), the glycosylation of EGCG has been explored by several groups, mostly by the use of enzymatic catalysis (37–39). Recently, our group reported the enzymatic synthesis of various α-glucosyl derivatives of EGCG by a transglycosylation reaction catalyzed by a cyclodextrin glucanotransferase (CGTase, EC 2.4.1.19) (40). Two main α-D-glucosides of EGCG were isolated and chemically characterized: EGCG 3′-O-α-D-glucopyranoside ( 1 ) and EGCG 7-O-α-D-glucopyranoside ( 2 ).…”

Section: Introductionmentioning

confidence: 99%

Effect of α-Glucosylation on the Stability, Antioxidant Properties, Toxicity, and Neuroprotective Activity of (–)-Epigallocatechin Gallate

et al. 2019

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(–)-Epigallocatechin gallate (EGCG), the predominant catechin (≥50%) in green tea ( Camellia sinensis ), displays several bioactive properties but its stability and bioavailability are low. In this work, the properties of two α-glucosyl derivatives of EGCG (3′- and 7-O-α-D-glucopyranoside), obtained by enzymatic synthesis, were assessed. The α-glucosylation enhanced the pH and thermal stability of EGCG. The analysis of scavenging activity toward ABTS · + radicals showed that the α-glucosylation at C-7 of A-ring caused a higher loss of antioxidant activity compared with the sugar conjugation at C-3′ of B-ring. The 3′-glucoside also showed higher potential to alleviate intracellular reactive oxygen species (ROS) levels and to boost REDOX activity. The toxicity of EGCG and its monoglucosides was tested in human SH-S5Y5 neurons, RAW 264.7 macrophages, MRC5 fibroblasts, and HT-29 colon cancer cells. Interestingly, the 3′-O-α-D-glucoside increased the viability of neural cells in vitro (2.75-fold at 100 μM) in the presence of H 2 O 2 , whilst EGCG gave rise only to a 1.7-fold enhancement. In conclusion, the α-glucoside of EGCG at C-3′ has a great potential for nutraceutical, cosmetic and biomedical applications.

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“…The enzyme CGTase has proved an exceptional capability to glucosylate compounds of different nature employing starch, maltodextrins, or cyclodextrins as glucosyl donors [9,10]. Apart from monosaccharides and disaccharides [11,12], other compounds such as flavonoids [13,14], vitamins [15], sugar alcohols [16], sweet glycosides [17], and polyols [18] have been successfully used as acceptor molecules for the intermolecular transglycosylation. Unfortunately, one of the main drawbacks of CGTases is that their product selectivity is not very high, because the enzyme displays its four activities simultaneously [19].…”

Section: Introductionmentioning

confidence: 99%

Production and Surfactant Properties of Tert-Butyl α-d-Glucopyranosides Catalyzed by Cyclodextrin Glucanotransferase

et al. 2019

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While testing the ability of cyclodextrin glucanotransferases (CGTases) to glucosylate a series of flavonoids in the presence of organic cosolvents, we found out that this enzyme was able to glycosylate a tertiary alcohol (tert-butyl alcohol). In particular, CGTases from Thermoanaerobacter sp. and Thermoanaerobacterium thermosulfurigenes EM1 gave rise to the appearance of at least two glycosylation products, which were characterized by mass spectrometry (MS) and nuclear magnetic resonance (NMR) as tert-butyl-α-D-glucoside (major product) and tert-butyl-α-D-maltoside (minor product). Using partially hydrolyzed starch as glucose donor, the yield of transglucosylation was approximately 44% (13 g/L of tert-butyl-α-D-glucoside and 4 g/L of tert-butyl-α-D-maltoside). The synthesized tert-butyl-α-D-glucoside exhibited the typical surfactant behavior (critical micellar concentration, 4.0–4.5 mM) and its properties compared well with those of the related octyl-α-D-glucoside. To the best of our knowledge, this is the first description of an enzymatic α-glucosylation of a tertiary alcohol.

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Efficient α-Glucosylation of Epigallocatechin Gallate Catalyzed by Cyclodextrin Glucanotransferase from Thermoanaerobacter Species

Cited by 22 publications

References 59 publications

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

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

Effect of α-Glucosylation on the Stability, Antioxidant Properties, Toxicity, and Neuroprotective Activity of (–)-Epigallocatechin Gallate

Production and Surfactant Properties of Tert-Butyl α-d-Glucopyranosides Catalyzed by Cyclodextrin Glucanotransferase

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