Synthesis and characterization of hydroquinone glucoside using Leuconostoc mesenteroides dextransucrase

Seo, Eun-Seong; Kang, Jin; Lee, Jin Ha; Kim, Go-Eun; Kim, Ghahyun J.; Kim, Doman

doi:10.1016/j.enzmictec.2009.07.011

Cited by 45 publications

(48 citation statements)

References 36 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In general, two approaches were employed. One was to use whole cells such as Xanthomonas campestris and B. subtilis, and the other was to employ carbohydrate-active enzymes, including α-glucosidase, sucrose phosphorylase, and dextransucrase (Kitao and Sekine 1994;Nishimura et al 1994;Kurosu et al 2002;Prodanovic et al 2005;Seo et al 2009b). Nishimura et al screened 600 strains of soil microorganisms for the production of HQ glucosylating enzyme (HGE) and selected B. subtilis strain X-23, which produced an enzyme that glucosylated HQ.…”

Section: Discussionmentioning

confidence: 99%

“…Nishimura et al first reported enzymatic synthesis of α-Ab with maltopentaose as a donor and HQ as an acceptor using α-amylase from Bacillus subtilis X-23 (1994). However, in most cases, several drawbacks were uncovered, such as relatively expensive substrate and low bioconversion yield (Nishimura et al 1994;Kurosu et al 2002;Prodanovic et al 2005;Seo et al 2009b). …”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

High-yield enzymatic bioconversion of hydroquinone to α-arbutin, a powerful skin lightening agent, by amylosucrase

Seo

Jung

et al. 2012

Appl Microbiol Biotechnol

View full text Add to dashboard Cite

α-Arbutin (α-Ab) is a powerful skin whitening agent that blocks epidermal melanin biosynthesis by inhibiting the enzymatic oxidation of tyrosine and L-3,4-dihydroxyphenylalanine (L-DOPA). α-Ab was effectively synthesized from hydroquinone (HQ) by enzymatic biotransformation using amylosucrase (ASase). The ASase gene from Deinococcus geothermalis (DGAS) was expressed and efficiently purified from Escherichia coli using a constitutive expression system. The expressed DGAS was functional and performed a glycosyltransferase reaction using sucrose as a donor and HQ as an acceptor. The presence of a single HQ bioconversion product was confirmed by thin-layer chromatography (TLC) and high-performance liquid chromatography (HPLC). The HQ bioconversion product was isolated by silica gel open column chromatography and its chemical structure determined by 1H and 13C nuclear magnetic resonance (NMR). The product was determined to be hydroquinone-O-α-D-glucopyranoside with a glucose molecule linked to HQ through an α-glycosidic bond. However, the production yield of the transfer reaction was significantly low (1.3%) due to the instability of HQ in the reaction mixture. The instability of HQ was considerably improved by antioxidant agents, particularly ascorbic acid, implying that HQ is labile to oxidation. A maximum yield of HQ transfer product of 90% was obtained at a 10:1 molar ratio of donor (sucrose) and acceptor (HQ) molecules in the presence of 0.2 mM ascorbic acid.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

High-yield enzymatic bioconversion of hydroquinone to α-arbutin, a powerful skin lightening agent, by amylosucrase

Seo

Jung

et al. 2012

Appl Microbiol Biotechnol

View full text Add to dashboard Cite

show abstract

“…Due to these disadvantages, the uses of EGCG in the food, drug, and cosmetic industries remains somewhat limited. To circumvent these disadvantages, enzymatic transglycosylation using Leuconostoc mesenteroides glucansucrases has been applied to the modification of EGCG and a variety of nature bioactive substances to improve their functionality and physicochemical properties [9][10][11]. Transglycosylated compounds display enhanced functionalities in water solubility, light stability, increased resistance to oxidation, and less bitter taste [9][10][11][12].…”

Section: Introductionmentioning

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

Self Cite

View full text Add to dashboard Cite

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.

show abstract

“…Sucrose phosphorylase (SP) is an attractive biocatalyst that can transfer a glucosyl moiety from sucrose or α‐ d ‐glucose‐1‐phosphate to a variety of acceptors, including mono‐, di‐ and trisaccharides, sugar alcohols and even phenolic compounds, to produce the corresponding glycosylated compounds. When the acceptor is hydroquinone, the commercially useful cosmetic ingredient α‐arbutin can be synthesized . α‐Arbutin is a potent inhibitor of tyrosinase, a critical enzyme for the generation of pigments: its use prevents melanin formation and has a whitening effect on the skin .…”

Section: Introductionmentioning

confidence: 99%

“…When the acceptor is hydroquinone, the commercially useful cosmetic ingredient -arbutin can be synthesized. [13][14][15] -Arbutin is a potent inhibitor of tyrosinase, a critical enzyme for the generation of pigments: its use prevents melanin formation and has a whitening effect on the skin. 16,17 Native SP, which is naturally a cytosolic protein, has been found in many organisms, including Pseudomonas saccharophila, Leuconostoc mesenteroides, Streptococcus mutans, Bifidobacterium longum and Bifidobacterium adolescen.…”

Section: Introductionmentioning

confidence: 99%

Highly efficient extracellular expression of naturally cytoplasmic Leuconostoc mesenteroides sucrose phosphorylase

Tian

et al. 2018

J of Chemical Tech & Biotech

View full text Add to dashboard Cite

BACKGROUND We previously showed that extracellular production of naturally cytoplasmic proteins could be realized through co‐expression with phospholipase C (PLC), which enhances cell membrane permeability through limited hydrolysis of membrane phospholipids. Leuconostoc mesenteroides sucrose phosphorylase (SPLc), a naturally cytoplasmic enzyme, exhibits excellent properties for synthesis of α‐arbutin, but no systemic investigation of its preparation has thus far been reported. RESULTS Three PLCs were selected and expressed, without signal peptide, in Escherichia coli. More than 90% of the PLCs from Listeria monocytogenes and Bacillus cereus were present in the culture medium. When SPLc was co‐expressed with these PLCs, and the location of the PLC and SPLc genes in the co‐expression vector was optimized, the highest production was obtained when SPLc gene was inserted upstream of the B. cereus PLC gene, as in BL21(DE3)/pETDuet‐sp‐bcplc. SPLc production was then scaled up to a 3 L fermenter and fermentation conditions were optimized. When the initial medium contained 0.6 mmol L−1 ZnCl2 and protein expression was induced at a dry cell weight of 15 g L−1 by the addition of lactose at 0.2 g L−1 h−1 at 30 °C, the extracellular SPLc activity reached its highest level of 1445.1 U mL−1 This constituted 81.6% of total activity; the remainder of the enzyme (18.4%) remained inside the cells. CONCLUSION This is the first report describing extracellular expression of sucrose phosphorylase, and the highest yield ever reported was obtained. This provides the basis for industrial‐scale production and application of sucrose phosphorylase. It also provides a potential method for improving the production of other proteins and fine chemicals. © 2018 Society of Chemical Industry

show abstract

Synthesis and characterization of hydroquinone glucoside using Leuconostoc mesenteroides dextransucrase

Cited by 45 publications

References 36 publications

High-yield enzymatic bioconversion of hydroquinone to α-arbutin, a powerful skin lightening agent, by amylosucrase

High-yield enzymatic bioconversion of hydroquinone to α-arbutin, a powerful skin lightening agent, by amylosucrase

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

Highly efficient extracellular expression of naturally cytoplasmic Leuconostoc mesenteroides sucrose phosphorylase

Contact Info

Product

Resources

About