Production of 2-O-α-glucopyranosyl l-ascorbic acid from ascorbic acid and β-cyclodextrin using immobilized cyclodextrin glycosyltransferase

Prousoontorn, Manchumas Hengsakul; Pantatan, Supranee

doi:10.1007/s10847-006-9163-5

Cited by 21 publications

(8 citation statements)

References 24 publications

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“…However, the decrease in expressed activity with increasing enzyme concentration can be attributed to the oversaturation of the enzyme over the support surface. Moreover, high enzyme concentration clustered on the surface of the support can reduce enzyme activity, owing to limited active site accessibility and denaturation of the enzyme [114][115][116][117] . Furthermore, the immobilization protocol might distort the enzyme, when there are multi-interactions between the enzyme and the support.…”

Section: Resultsmentioning

confidence: 99%

Immobilization of alcohol dehydrogenase from Saccharomyces cerevisiae onto carboxymethyl dextran-coated magnetic nanoparticles: a novel route for biocatalyst improvement via epoxy activation

Vasić

Knez

Leitgeb

2020

Sci Rep

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A novel method is described for the immobilization of alcohol dehydrogenase (ADH) from Saccharomyces cerevisiae onto carboxymethyl dextran (CMD) coated magnetic nanoparticles (CMD-MNPs) activated with epoxy groups, using epichlorohydrin (EClH). EClH was used as an activating agent to bind ADH molecules on the surface of CMD-MNPs. Optimal immobilization conditions (activating agent concentration, temperature, rotation speed, medium pH, immobilization time and enzyme concentration) were set to obtain the highest expressed activity of the immobilized enzyme. ADH that was immobilized onto epoxy-activated CMD-MNPs (ADH-CMD-MNPs) maintained 90% of the expressed activity. Thermal stability of ADH-CMD-MNPS after 24 h at 20 °C and 40 °C yielded 79% and 80% of initial activity, respectively, while soluble enzyme activity was only 19% at 20 °C and the enzyme was non-active at 40 °C. Expressed activity of ADH-CMD-MNPs after 21 days of storage at 4 °C was 75%. Kinetic parameters (KM, vmax) of soluble and immobilized ADH were determined, resulting in 125 mM and 1.2 µmol/min for soluble ADH, and in 73 mM and 4.7 µmol/min for immobilized ADH.

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Section: Resultsmentioning

confidence: 99%

Immobilization of alcohol dehydrogenase from Saccharomyces cerevisiae onto carboxymethyl dextran-coated magnetic nanoparticles: a novel route for biocatalyst improvement via epoxy activation

Vasić

Knez

Leitgeb

2020

Sci Rep

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“…was studied (Jun et al 2001), and the amount of AA-2G produced was 2.987 g/L under optimal transformation conditions. Prousoontorn and Pantatan (2007) produced AA-2G using immobilized CGTase with alumina as the carrier. The yield of AA-2G was 2.92 % and the immobilized CGTase retained activity up to 74.4 % of its initial catalytic activity.…”

Section: Production Of Aa-2g By Biotransformationmentioning

confidence: 99%

Functions, applications and production of 2-O-d-glucopyranosyl-l-ascorbic acid

Han

Liu

et al. 2012

Appl Microbiol Biotechnol

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Vitamin C (VC) is an essential nutrient that cannot be synthesized by the human body. Due to its extreme instability, various VC derivatives have been developed in an attempt to improve stability while retaining the same biological activity. One of the most important VC derivatives, 2-O-D-glucopyranosyl-L-ascorbic acid (AA-2G), has attracted increasing attention in recent years with a wide range of applications in cosmetics, food, and medicine. In this mini-review, we first introduce the types and properties of different VC glycosyl derivatives. Next, we provide an overview of the functions and applications of AA-2G. Finally, we discuss in-depth the current status and future prospects of AA-2G production by biotransformation.

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“…Although AA-2G can be produced by different enzymes [11,13,14], but studies have shown that cyclodextrin glucanotransferase (CGTase) is the most preferable either mostly in free [15], immobilized [16], recombinant [17], or in mutant state [18]. CGTase transfer glucose unit to C 2 in AA via transglycosylation from glycosyl donor, different substrates were used as glycosyl donor except glucose [15,17].…”

Section: Introductionmentioning

confidence: 99%

Biosynthesis of 2-O-α-D-glucopyranosyl-L-Ascorbic Acid from Maltose by Cyclodextrin Glucanotransferase from Bacillus sp. SK 13.002

Eibaid¹,

Bashari²,

Miao³

et al. 2014

JFNR

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In this work 2-O-α-D-glucopyranosyl-L-ascorbic acid (AA-2G) was synthesized by Cyclodextrin glucanotransferase (CGTase) from Bacillus sp. SK 13.002 with L-ascorbic acid (AA) as an acceptor and maltose as a glycosyl donor. AA-2G production was analyzed by HPLC and was confirmed by LC/MS results. The reaction parameters, such as pH (4.0-9.0), temperature (25-50°C), time (0-30 h), substrate ratios and enzyme concentration were optimized. The results showed that the optimum condition was pH 8.0 at 37°C for 24 h, 1:1 maltose to AA substrates mass ratio, and 200 U/mL of CGTase. Under these conditions, the production of AA-2G was 5.5 g/L, this result indicate that CGTase from Bacillus sp. SK 13.002 can effectively uses maltose as a glycosyl donor to produce AA-2G in high yield.

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Production of 2-O-α-glucopyranosyl l-ascorbic acid from ascorbic acid and β-cyclodextrin using immobilized cyclodextrin glycosyltransferase

Cited by 21 publications

References 24 publications

Immobilization of alcohol dehydrogenase from Saccharomyces cerevisiae onto carboxymethyl dextran-coated magnetic nanoparticles: a novel route for biocatalyst improvement via epoxy activation

Immobilization of alcohol dehydrogenase from Saccharomyces cerevisiae onto carboxymethyl dextran-coated magnetic nanoparticles: a novel route for biocatalyst improvement via epoxy activation

Functions, applications and production of 2-O-d-glucopyranosyl-l-ascorbic acid

Biosynthesis of 2-O-α-D-glucopyranosyl-L-Ascorbic Acid from Maltose by Cyclodextrin Glucanotransferase from Bacillus sp. SK 13.002

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