Flavanone and isoflavone glucosylation by non-Leloir glycosyltransferases

Overwin, Heike; Wray, Victor; Seeger, Michael; Sepúlveda-Boza, Silvia; Höfer, Bernd

doi:10.1016/j.jbiotec.2016.06.026

Cited by 20 publications

(18 citation statements)

References 49 publications

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“…-taxifolin and luteolin were very low (5 and 7%, respectively). The NpAS transferred glucose from sucrose as a donor molecule to the 7 position of the A-ring in isoflavone as an acceptor molecule (Overwin et al, 2016). The conversion rate of NpAS for isoflavone was 60-70% higher than that of flavanonol and flavone.…”

Section: Synthesis Of Novel Functional Compounds Using Transglycosylamentioning

confidence: 97%

“…The NpAS transfected stereospecific glucosylation at the 4 0 -position in the B-ring of (? )-taxifolin and luteolin (these belong to flavanonol and flavone in the flavonoid, respectively) as an acceptor molecule (Malbert et al, 2014;Overwin et al, 2016). However, the bioconversion yields of (?)…”

Section: Synthesis Of Novel Functional Compounds Using Transglycosylamentioning

confidence: 99%

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Versatile biotechnological applications of amylosucrase, a novel glucosyltransferase

Seo

Yoo

Choi

et al. 2020

Food Sci Biotechnol

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Amylosucrase (AS; EC 2.4.1.4) is an enzyme that has great potential in the biotechnology and food industries, due to its multifunctional enzyme activities. It can synthesize a-1,4-glucans, like amylose, from sucrose as a sole substrate, but importantly, it can also utilize various other molecules as acceptors. In addition, AS produces sucrose isomers such as turanose and trehalulose. It also efficiently synthesizes modified starch with increased ratios of slow digestive starch and resistant starch, and glucosylated functional compounds with increased water solubility and stability. Furthermore, AS produces turnaose more efficiently than other carbohydrate-active enzymes. Amylose synthesized by AS forms microparticles and these can be utilized as biocompatible materials with various bio-applications, including drug delivery, chromatography, and bioanalytical sciences. This review not only compares the gene and enzyme characteristics of microbial AS, studied to date, but also focuses on the applications of AS in the biotechnology and food industries.

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Section: Synthesis Of Novel Functional Compounds Using Transglycosylamentioning

confidence: 97%

Section: Synthesis Of Novel Functional Compounds Using Transglycosylamentioning

confidence: 99%

Versatile biotechnological applications of amylosucrase, a novel glucosyltransferase

Seo

Yoo

Choi

et al. 2020

Food Sci Biotechnol

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“…Amylosucrase (AS) is a glycosyltransferase (GT) structurally belonging to the glycoside hydrolase [1,2]. Transglycosylation reactions of AS are usually conjugations of single and/or multiple (gluco-oligosaccharides) sugar(s) with a great advantage compared with Leloir GTs.…”

Section: Introductionmentioning

confidence: 99%

“…Transglycosylation reactions of AS are usually conjugations of single and/or multiple (gluco-oligosaccharides) sugar(s) with a great advantage compared with Leloir GTs. For production of bioactive phenolic glycosides [2,3], AS has been used in the synthesis of a variety of attractive biomaterials including amylose-like polymers, starch, dendritic nanoparticles, and microparticle encapsulation [4][5][6]. Although AS has potential application in glycodiversification, it is rarely reported for transglycosyation of phenolic compounds.…”

Section: Introductionmentioning

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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“…Glycosylation modulates the solubility, bioavailability, and chemical properties of many natural products, such as flavonoids and steroids [7]. Many novel bioactive flavonoid glycosides have been obtained by enzymatic glycosylation for developing new and potential drugs [8].…”

Section: Introductionmentioning

confidence: 99%

Enzymatic Synthesis of Novel and Highly Soluble Puerarin Glucoside by Deinococcus geothermalis Amylosucrase

Ding

Wang

et al. 2022

Molecules

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Puerarin (daidzein-8-C-glucoside) is an isoflavone isolated from several leguminous plants of the genus Pueraria. Puerarin possesses several pharmacological properties; however, the poor solubility of puerarin limits its applications. To resolve this poor solubility, Deinococcus geothermalis amylosucrase (DgAS) was used to modify puerarin into more soluble derivatives. The results showed that DgAS could biotransform puerarin into a novel compound: puerarin-4′-O-α-glucoside. The biotransformation reaction was manipulated at different temperatures, pH values, sucrose concentrations, reaction times, and enzyme concentrations. The results showed that the optimal reaction condition was biotransformed by 200 μg/mL DgAS with 20% (w/v) sucrose at pH 6 and incubated at 40 °C for 48 h, and the optimal production yield was 35.1%. Puerarin-4′-O-α-glucoside showed 129-fold higher solubility than that of puerarin and, thus, could be further applied for pharmacological use in the future.

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Flavanone and isoflavone glucosylation by non-Leloir glycosyltransferases

Cited by 20 publications

References 49 publications

Versatile biotechnological applications of amylosucrase, a novel glucosyltransferase

Versatile biotechnological applications of amylosucrase, a novel glucosyltransferase

Sustainable Production of Dihydroxybenzene Glucosides Using Immobilized Amylosucrase from Deinococcus geothermalis

Enzymatic Synthesis of Novel and Highly Soluble Puerarin Glucoside by Deinococcus geothermalis Amylosucrase

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