Transglucosylation of hydroquinone catalysed by α-glucosidase from baker's yeast

Prodanović, Radivoje; Milosavić, Nenad; Sladić, Dušan; Zlatović, Mario; Božić, Branislav; Veličković, Tanja Ćirković; Vujčić, Zoran

doi:10.1016/j.molcatb.2005.06.011

Cited by 52 publications

(31 citation statements)

References 16 publications

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“…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%

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

Seo

Jung

et al. 2012

Appl Microbiol Biotechnol

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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.

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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

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“…For example, the α-glucosidase from Aspergillus niger converted maltose into isomaltose and panose (Duan et al 1995) and that from Xantophyllomyces dendrorhous yielded a final product enriched in trisaccharides and tetrasaccharides (Lucia et al 2007). This transglycosylation activity has been applied in the industrial production of isomaltooligodaccharides (Crittenden & Playne 1996) and in improving the chemical properties by conjugating sugar residues (Murase et al 1997;Prodanovic et al 2005).…”

Section: Introductionmentioning

confidence: 99%

Expression and characterization of an α-glucosidase from Thermoanaerobacter ethanolicus JW200 with potential for industrial application

et al. 2009

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In this study, a new α-glucosidase gene from Thermoanaerobacter ethanolicus JW200 was cloned and expressed in Escherichia coli by a novel heat-shock vector pHsh. The recombinant α-glucosidase exhibited its maximum hydrolytic activity at 70• C and pH 5.0∼5.5. With p-nitrophenyl-α-D-glucoside as a substrate and under the optimal condition (70 • C, pH 5.5), Km and Vmax of the enzyme was 1.72 mM and 39 U/mg, respectively. The purified α-glucosidase could hydrolyze oligosaccharides with both α-1,4 and α-1,6 linkages. The enzyme also had strong transglycosylation activity when maltose was used as sugar donor. The transglucosylation products towards maltose are isomaltose, maltotriose, panose, isomaltotriose and tetrasaccharides. The enzyme could convert 400 g/L maltose to oligosaccharides with a conversion rate of 52%, and 83% of the oligosaccharides formed were prebiotic isomaltooligosaccharides (containing isomaltose, panose and isomaltotriose).

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“…those from Aspergillus niger [14], Bacillus stearothermophilus [15], S. cerevisiae [16] or brewer's yeast [15]. This transglycosylation activity is being applied to produce prebiotic isomaltooligosaccharides [17,18] or to glucosylate compounds such as L-menthol [15], pyridoxine [19] and hydroquinone [20]. The basidiomycetous yeast Xanthophyllomyces dendrorhous (formerly Phaffia rhodozyma) was isolated from deciduous trees [21], and it produces astaxanthin (3-3 0 -dihydroxi-b,b-carotene-4,4-dione) as the main carotenoid [22].…”

Section: Introductionmentioning

confidence: 99%

Transformation of maltose into prebiotic isomaltooligosaccharides by a novel α-glucosidase from Xantophyllomyces dendrorhous

Fernández‐Arrojo

Marín

Segura

et al. 2007

Process Biochemistry

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The transglycosylation activity of a novel a-glucosidase from the basidiomycetous yeast Xanthophyllomyces dendrorhous (formerly Phaffia rhodozyma) was studied using maltose as glucosyl donor. The enzyme synthesized oligosaccharides with a-(1 ! 2), a-(1 ! 4) and a-(1 ! 6) bonds. Using 200 g/l maltose, the yield of oligosaccharides was 53.8 g/l, with prebiotic oligosaccharides containing at least one a-(1 ! 6) linkage (panose, 6-O-a-glucosyl-maltotriose and 6-O-a-isomaltosyl-maltose) being the major products (47.1 g/l). The transglycosylatying yield was 3.6 times higher than the observed with the a-glucosidase from Saccharomyces cerevisiae (53.8 vs. 14.7 g/l). Moreover, when increasing the maltose concentration up to 525 g/l, the maximum production of tri-and tetrasaccharides reached 167.1 g/l, without altering the percentage of oligosaccharides in the mixture. Compared with other microbial a-glucosidases in which the main transglycosylation product is a disaccharide, the enzyme from X. dendrorhous yields a final product enriched in trisaccharides and tetrasaccharides. #

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Transglucosylation of hydroquinone catalysed by α-glucosidase from baker's yeast

Cited by 52 publications

References 16 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

Expression and characterization of an α-glucosidase from Thermoanaerobacter ethanolicus JW200 with potential for industrial application

Transformation of maltose into prebiotic isomaltooligosaccharides by a novel α-glucosidase from Xantophyllomyces dendrorhous

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