Production of Epigallocatechin Gallate 7-O-α-D-Glucopyranoside (EGCG-G1) Using the Glucosyltransferase from Leuconostoc mesenteroides

Hyun, Eun-Kyung; Park, Ha Young; Kim, Hye-jung; Lee, Jung-Kul; Kim, Doman; Oh, Deok-Kun

doi:10.1021/bp0700657

Cited by 4 publications

(4 citation statements)

References 30 publications

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“…However, their antioxidant activity remained unchanged or was slightly lower. Hyun et al further optimized the reaction conditions for the synthesis of EGCG-G1 using glucansucrase of L. mesenteroides B-1299CB as catalyst, achieving a conversion efficiency of 67% under optimized conditions (Hyun et al 2007). Glucansucrase of L. mesenteroides B-1299CB was also demonstrated to glucosylate quercetin with the production of α-D-glucopyranosyl-4′-O-quercetin and α-D-glucopyranosyl-3′-O-quercetin (Figure 7), whose solubility in water were significantly improved ).…”

Section: Glucosylation Of Flavonoids By Glucansucrasesmentioning

confidence: 99%

“…However, glucansucrases were also capable of glucosylating the hydroxyl group on the A ring of flavonoids (hydroxyl group at position 7). Hyun et al, showed that the glucansucrase of L. mesenteroides B-1299CB used EGCG as the acceptor subs t r a t e t o c a t a l y z e t h e s y n t h e s i s o f α-D-glucopyranosyl-7-O-EGCG with a conversion degree of 67% (Hyun et al 2007). GtfR of S. oralis was reported to specifically attach a glucosyl moiety to the flavanone compound taxifolin at the para position (O4') of the B ring while it transferred a glucosyl moiety to the C7 hydroxyl group of the A ring of isoflavones (Overwin et al 2016).…”

Section: Glucosylation Of Flavonoids By Glucansucrasesmentioning

confidence: 99%

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Enzymatic glucosylation of polyphenols using glucansucrases and branching sucrases of glycoside hydrolase family 70

Meng

Leeuw³

et al. 2021

Critical Reviews in Food Science and Nutrition

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Polyphenols exhibit various beneficial biological activities and represent very promising candidates as active compounds for food industry. However, the low solubility, poor stability and low bioavailability of polyphenols have severely limited their industrial applications. enzymatic glycosylation is an effective way to improve the physicochemical properties of polyphenols. As efficient transglucosidases, glycoside hydrolase family 70 (GH70) glucansucrases naturally catalyze the synthesis of polysaccharides and oligosaccharides from sucrose. Notably, GH70 glucansucrases show broad acceptor substrate promiscuity and catalyze the glucosylation of a wide range of non-carbohydrate hydroxyl group-containing molecules, including benzenediol, phenolic acids, flavonoids and steviol glycosides. Branching sucrase enzymes, a newly established subfamily of GH70, are shown to possess a broader acceptor substrate binding pocket that acts efficiently for glucosylation of larger size polyphenols such as flavonoids. Here we present a comprehensive review of glucosylation of polyphenols using GH70 glucansucrase and branching sucrases. Their catalytic efficiency, the regioselectivity of glucosylation and the structure of generated products are described for these reactions. Moreover, enzyme engineering is effective for improving their catalytic efficiency and product specificity. The combined information provides novel insights on the glucosylation of polyphenols by GH70 glucansucrases and branching sucrases, and may promote their applications.

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Section: Glucosylation Of Flavonoids By Glucansucrasesmentioning

confidence: 99%

Section: Glucosylation Of Flavonoids By Glucansucrasesmentioning

confidence: 99%

Enzymatic glucosylation of polyphenols using glucansucrases and branching sucrases of glycoside hydrolase family 70

Meng

Leeuw³

et al. 2021

Critical Reviews in Food Science and Nutrition

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“…The acceptor reaction mediated by L. mesenteroides glucosyltransferase and purification of EGCG-G1 using Sephadex LH-20 chromatography were performed as described previously [9,19].…”

Section: Preparation Of Egcg-g1mentioning

confidence: 99%

Inhibitory effects of epigallocatechin gallate and its glucoside on the human intestinal maltase inhibition

Nguyen

Jung

Lee

et al. 2012

Biotechnol Bioproc E

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Human intestinal maltase (HMA) is an αglucosidase responsible for the hydrolysis of α-1,4-linkages from the non-reducing end of malto-oligosaccharides. HMA has become an important target in the treatment of type-2 diabetes. In this study, epigallocatechin gallate (EGCG) and EGCG glucoside (EGCG-G1) were identified as inhibitors of HMA by an in vitro assay with IC 50 of 20 ± 1.0 and 31.5 ± 1.0 µM, respectively. A Lineweaver-Burk plot confirmed that EGCG and EGCG-G1 were competitive inhibitors of maltose substrate against HMA and inhibition kinetic constants (K i ) calculated from a Dixon plot were 5.93 ± 0.26 and 7.88 ± 0.57 µM, respectively. Both EGCG and EGCG-G1 bound to the active site of HMA with numerous hydrophobic and hydrogen bond interactions.

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“…In comparison, the glucosylated flavanol gallates exhibit similar antioxidant properties, yet have increased solubility in water and stronger tyrosinase inhibitory effects, suggesting that these forms may be superior to flavanol gallates aglycones for application as food additives, drugs, and cosmetics ( Moon et al, 2006 ; Zhang et al, 2016 ). To date, glycosylation of flavan-3-ols gallates have often been carried out via chemical conversion or use of glycosyltransferases of bacterial origin ( Kitao et al, 1995 ; Moon et al, 2006 ; Hyun et al, 2007 ; Zhang et al, 2016 ).…”

Section: Discussionmentioning

confidence: 99%

Characterization of UGT716A1 as a Multi-substrate UDP:Flavonoid Glucosyltransferase Gene in Ginkgo biloba

Shen

et al. 2017

Front. Plant Sci.

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Ginkgo biloba L., a “living fossil” and medicinal plant, is a well-known rich source of bioactive flavonoids. The molecular mechanism underlying the biosynthesis of flavonoid glucosides, the predominant flavonoids in G. biloba, remains unclear. To better understand flavonoid glucosylation in G. biloba, we generated a transcriptomic dataset of G. biloba leaf tissue by high-throughput RNA sequencing. We identified 25 putative UDP-glycosyltransferase (UGT) unigenes that are potentially involved in the flavonoid glycosylation. Among them, we successfully isolated and expressed eight UGT genes in Escherichia coli, and found that recombinant UGT716A1 protein was active toward broad range of flavonoid/phenylpropanoid substrates. In particular, we discovered the first recombinant UGT protein, UGT716A1 from G. biloba, possessing unique activity toward flavanol gallates that have been extensively documented to have significant bioactivity relating to human health. UGT716A1 expression level paralleled the flavonoid distribution pattern in G. biloba. Ectopic over-expression of UGT716A1 in Arabidopsis thaliana led to increased accumulation of several flavonol glucosides. Identification and comparison of the in vitro enzymatic activity of UGT716A1 homologs revealed a UGT from the primitive land species Physcomitrella patens also showed broader substrate spectrum than those from higher plants A. thaliana, Vitis vinifera, and Medicago truncatula. The characterization of UGT716A1 from G. biloba bridges a gap in the evolutionary history of UGTs in gymnosperms. We also discuss the implication of UGT716A1 for biosynthesis, evolution, and bioengineering of diverse glucosylated flavonoids.

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Production of Epigallocatechin Gallate 7-O-α-D-Glucopyranoside (EGCG-G1) Using the Glucosyltransferase from Leuconostoc mesenteroides

Cited by 4 publications

References 30 publications

Enzymatic glucosylation of polyphenols using glucansucrases and branching sucrases of glycoside hydrolase family 70

Enzymatic glucosylation of polyphenols using glucansucrases and branching sucrases of glycoside hydrolase family 70

Inhibitory effects of epigallocatechin gallate and its glucoside on the human intestinal maltase inhibition

Characterization of UGT716A1 as a Multi-substrate UDP:Flavonoid Glucosyltransferase Gene in Ginkgo biloba

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