Enzymatic synthesis and characterization of novel epigallocatechin gallate glucosides

Moon, Yea Hwang; Kim, Ghahyun; Lee, Jin Ha; Jin, Xing-Ji; Kim, Do-Won; Kim, Doman

doi:10.1016/j.molcatb.2006.01.030

Cited by 28 publications

(31 citation statements)

References 29 publications

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“…Among the EGCG glucosides, EGCG-G1 has attracted the most attention as a novel compound because EGCG-G1 showed higher water solubility and stability and similar antioxidant effect compared with EGCG. On the other hand, the other EGCG glucosides exhibited lower antioxidant effects compared with EGCG (21,23).…”

Section: Introductionmentioning

confidence: 88%

“…To overcome these disadvantages, the glycosylation of catechins has been attempted using microbial enzymes of Arthrobacter sp. (19), Bacillus subtilis X-23 (20), Leuconostoc mesenteroides B-1299CB (21), and Xathomonas campestris WU-9701 (22). The glycosylated compounds exhibited improved water solubility, stability, taste, and tyrosinase inhibition (19)(20)(21)(22)(23)(24)(25).…”

Section: Introductionmentioning

confidence: 99%

“…The glucosylation of EGCG to improve its properties was performed by a glucosyltransferase from L. mesenteroides B-1299CB (21,23). The EGCG glucosides synthesized by the glucosyltransferase with EGCG and sucrose were identified as epigallocatechin (Figures 1 and 2).…”

Section: Introductionmentioning

confidence: 99%

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

et al. 2007

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Epigallocatechin gallate 7-O-alpha-D-glucopyranoside (EGCG-G1), as a novel compound with a higher water solubility and stability and similar antioxidant effect when compared with epigallocatechin gallate (EGCG), was produced from sucrose as a glucose donor and EGCG as a glucose acceptor by a glucosyltransferase from Leuconostoc mesenteroides. The pH and temperature for maximum EGCG-G1 production by the glucosyltransferase were 5.0 and 25 degrees C, respectively. The enzyme and substrates concentrations to produce maximum EGCG-G1 were 3.78 units/mL, 25 mM sucrose, and 1.5 mM EGCG, respectively. Under these conditions, the glucosyltransferase produced 1.0 mM EGCG-G1 from 1.5 mM EGCG at a reaction time of 180 min, corresponding to formation of 67% product on a mole basis.

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Section: Introductionmentioning

confidence: 88%

Section: Introductionmentioning

confidence: 99%

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

et al. 2007

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“…Studies on the transglucosylation reactions of CGTases have been reported, as well as for the other sugar transferases, such as the glucosidases and glucansucrases [8][9][10]. For CGTase, transglucosylation occurs when either starch or cyclodextrin is used as the glucosyl donor.…”

Section: Introductionmentioning

confidence: 99%

“…It is well recognized that transglycosylation can often result in new properties of the glycosylated recipient compounds. The glycoside products usually show significantly improved functionalities such as improved sweetness, increased water solubility, increased stability against chemical agents or stimulating growth of Bifidobacteria [10]. For example, the solubility of neohesperidin glucoside in water is 1500 times higher than that of neohesperidin and the bitterness of the glucoside form was 10 times less than its parent neohesperidin [4].…”

Section: Introductionmentioning

confidence: 99%

Synthesis of cellobiose-containing oligosaccharides by intermolecular transglucosylation of cyclodextrin glycosyltransferase from Paenibacillus sp. A11

Wongsangwattana

Kaulpiboon

et al. 2010

Process Biochemistry

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Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for the period 2005–2006

Harvey

2010

Mass Spectrometry Reviews

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This review is the fourth update of the original review, published in 1999, on the application of MALDI mass spectrometry to the analysis of carbohydrates and glycoconjugates and brings coverage of the literature to the end of 2006. The review covers fundamental studies, fragmentation of carbohydrate ions, method developments, and applications of the technique to the analysis of different types of carbohydrate. Specific compound classes that are covered include carbohydrate polymers from plants, N- and O-linked glycans from glycoproteins, glycated proteins, glycolipids from bacteria, glycosides, and various other natural products. There is a short section on the use of MALDI-TOF mass spectrometry for the study of enzymes involved in glycan processing, a section on industrial processes, particularly the development of biopharmaceuticals and a section on the use of MALDI-MS to monitor products of chemical synthesis of carbohydrates. Large carbohydrate-protein complexes and glycodendrimers are highlighted in this final section.

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Enzymatic synthesis and characterization of novel epigallocatechin gallate glucosides

Cited by 28 publications

References 29 publications

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

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

Synthesis of cellobiose-containing oligosaccharides by intermolecular transglucosylation of cyclodextrin glycosyltransferase from Paenibacillus sp. A11

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for the period 2005–2006

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