Enzymatic biosynthesis of novel bavachin glucosides via Bacillus UDP-glycosyltransferase

Dai, Yiqun; Zhang, Songsong; Liu, Dachuan; Hong-mei, LI; Ma, Tao; Huo, Qiang; Wu, Cheng‐Zhu

doi:10.1016/j.phytol.2017.11.005

Cited by 11 publications

(5 citation statements)

References 17 publications

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“…Known for the substrate promiscuity, YjiC glucosyltransferase (Pandey et al 2014 ; Bashyal et al 2020 ) was employed in several studies, where various pH values were tested. Interestingly, the product distribution of glycosylation conducted by YjiC slightly varies in different pH (Dai et al 2018 ; Thapa et al 2019 ), which was not observed within this research, due to the structure of substrates used, with single hydroxyl moieties available for the glucosylation. However, in most cases, a pH of 7.5 was employed as the best environment for the YjiC activity (Parajuli et al 2014 ; Kim et al 2018 ).…”

Section: Discussionmentioning

confidence: 61%

Evaluation of double expression system for co-expression and co-immobilization of flavonoid glucosylation cascade

Matera

Dulak

Sordon

et al. 2022

Appl Microbiol Biotechnol

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Glucosylation cascade consisting of Leloir glycosyltransferase and sucrose synthase with in situ regeneration system of expensive and low available nucleotide sugars is a game-changing strategy for enzyme-based production of glycoconjugates of relevant natural products. We designed a stepwise approach including co-expression and one-step purification and co-immobilization on glass-based EziG resins of sucrose synthase from Glycine max (GmSuSy) with promiscuous glucosyltransferase YjiC from Bacillus licheniformis to produce efficient, robust, and versatile biocatalyst suited for preparative scale flavonoid glucosylation. The undertaken investigations identified optimal reaction conditions (30 °C, pH 7.5, and 10 mM Mg2+) and the best-suited carrier (EziG Opal). The prepared catalyst exhibited excellent reusability, retaining up to 96% of initial activity after 12 cycles of reactions. The semi-preparative glucosylation of poorly soluble isoflavone Biochanin A resulted in the production of 73 mg Sissotrin (Biochanin A 7-O-glucoside). Additionally, the evaluation of the designed double-controlled, monocistronic expression system with two independently induced promoters (rhaBAD and trc) brought beneficial information for dual-expression plasmid design. Key points • Simultaneous and titratable expression from two independent promoters is possible, although full control over the expression is limited. • Designed catalyst managed to glucosylate poorly soluble isoflavone. • The STY of Sissotrin using the designed catalyst reached 0.26 g/L∙h∙g of the resin. Graphical Abstract

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Section: Discussionmentioning

confidence: 61%

Evaluation of double expression system for co-expression and co-immobilization of flavonoid glucosylation cascade

Matera

Dulak

Sordon

et al. 2022

Appl Microbiol Biotechnol

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“…The Leloir glycosyltransferases use sugar nucleotides as activated donors when catalyze the transglycosylation reaction. For example, UDP-glycosyltransferase is a Leloir glycosyltransferase that catalyzes transglycosylation reaction by transferring glycosyl groups from activated donors, such as uridine diphospho-D-glucose, to acceptors [ 25 ]. On the other hand, non-Leloir glycosyltransferases use either sugar phosphates or non-activated sugars as donors when catalyze transglycosylation reaction.…”

Section: Importance Of Enzymatic Transglycosylationmentioning

confidence: 99%

Comprehensive study on transglycosylation of CGTase from various sources

Lim

Rasti

Sulistyo

et al. 2021

Heliyon

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Transglycosylation is the in-vivo or in-vitro process of transferring glycosyl groups from a donor to an acceptor, which is usually performed by enzymatic reactions because of their simplicity, low steric hindrance, high region-specificity, low production cost, and mild processing conditions. One of the enzymes commonly used in the transglycosylation reaction is cyclodextrin glucanotransferase (CGTase). The transglycosylated products, catalyzed by CGTase, are widely used in food additives, supplements, and personal care and cosmetic products. This is due to improvements in the solubility, stability, bioactivity and length of the synthesized products. This paper's focus is on the importance of enzymes used in the transglycosylation reaction, their characteristics and mechanism of action, sources and production yield, and donor and acceptor specificities. Moreover, the influence of intrinsic and extrinsic factors on the enzymatic reaction, catalysis of glycosidic linkages, and advantages of CGTase transglycosylation reactions are discussed in detail.

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“…It is reported that some cytotoxic glycoside exhibit less anticancer potential in vitro than the corresponding aglycone or after being inactivated by glycosylation. 20,21) Therefore, further studies on the in vivo anticancer activity and pharmacokinetic properties of shikonin glucosides 1 and 2 are required to fully understand their potential as therapeutic agents. Enzymatic Glycosylation and Purification of Shikonin Glucosides Incubation time, buffer pH, and concentration of UDP-Glc were investigated to optimize the different parameters in reactions as previously described.…”

Section: Determination Of Ph and Temperature Stabilitymentioning

confidence: 99%

“…Enzymatic Glycosylation and Purification of Shikonin Glucosides Incubation time, buffer pH, and concentration of UDP-Glc were investigated to optimize the different parameters in reactions as previously described. 22) The optimal glucosylation reaction was performed in a 50 mL reaction vessel containing 100 mM of Tris-HCl (pH 6), 1 mM of MgCl 2 , 1.5 mM of shikonin, 3 mM of UDP-Glc, and 50 µg/mL of YjiC enzyme, which was incubated at 28°C for 6 h. The reaction mixture was extracted with EtOAc and the extract was purified by semi-prep HPLC with 25% acetonitrile in water (3.0 mL/min) to yield compounds 1 (4.3 mg) and 2 (14.1 mg), respectively.…”

Section: Determination Of Ph and Temperature Stabilitymentioning

confidence: 99%

Biosynthesis of Novel Shikonin Glucosides by Enzymatic Glycosylation

Zhu

et al. 2019

CHEMICAL & PHARMACEUTICAL BULLETIN

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Shikonin, a natural naphthoquinone, has attracted much attention due to its various biological activities. Two shikonin glucosides, shikonin-1′,8-di-O-β-D-glucopyranoside (1) and shikonin-1′-O-β-D-glucopyranoside (2), were biosynthesized through in vitro enzymatic glycosylation and their structures were elucidated using spectroscopic techniques. The water-solubility and stability of compounds 1 and 2 were significantly higher than those of the parent compound. Furthermore, compound 2 showed moderate cytotoxicity against six cancer cell lines, with IC 50 values ranging from 36.10 to 67.47 µM. This research indicated that in vitro enzymatic glycosylation of shikonin is an effective strategy to improve it water solubility and chemical stability.

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Enzymatic biosynthesis of novel bavachin glucosides via Bacillus UDP-glycosyltransferase

Cited by 11 publications

References 17 publications

Evaluation of double expression system for co-expression and co-immobilization of flavonoid glucosylation cascade

Evaluation of double expression system for co-expression and co-immobilization of flavonoid glucosylation cascade

Comprehensive study on transglycosylation of CGTase from various sources

Biosynthesis of Novel Shikonin Glucosides by Enzymatic Glycosylation

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