The Cetus Process Revisited: A Novel Enzymatic Alternative for the Production of Aldose-Free D-Fructose

Leitner, Christian; Neuhauser, Wilfried; Volc, Jindřich; Kulbe, Klaus D.; Nidetzky, Bernd; Haltrich, Dietmar

doi:10.3109/10242429809003629

Cited by 49 publications

(32 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The lack of oxidation at position C-3 by T. multicolor P2O is an advantage when the conversion of pyranose sugars to their corresponding 2-keto derivatives is desired, such as in preparative biotransformations. The primary oxidation product of D-glucose has recently attracted increased attention due to its potential use as an intermediate in the production of aldose-free fructose (22,25,34).…”

Section: Discussionmentioning

confidence: 99%

“…Some of its properties, such as its high affinity for oxygen and its almost complete lack of activity with 2-deoxy-D-glucose, which is a common feature of other P2Os, should make the T. multicolor P2O an attractive biocatalyst for synthesis of 2-keto-D-glucose; the latter compound can be used as an intermediate for production of aldose-free fructose (34) or other ketoaldoses that are of interest for carbohydrate chemistry (21,22).…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Purification and Characterization of Pyranose Oxidase from the White Rot Fungus Trametes multicolor

Leitner¹,

Volc

Haltrich³

2001

Appl Environ Microbiol

Self Cite

146

166

View full text Add to dashboard Cite

We purified an intracellular pyranose oxidase from mycelial extracts of the white rot fungus Trametes multicolor by using ammonium sulfate fractionation, hydrophobic interaction, ion-exchange chromatography, and gel filtration. The native enzyme has a molecular mass of 270 kDa as determined by equilibrium ultracentrifugation and is composed of four identical 68-kDa subunits as determined by matrix-assisted laser desorption ionization mass spectrometry. Each subunit contains one covalently bound flavin adenine dinucleotide as its prosthetic group. The enzyme oxidizes several aldopyranoses specifically at position C-2, and its preferred electron donor substrates are D-glucose, D-xylose, and L-sorbose. During this oxidation reaction electrons are transferred to oxygen, yielding hydrogen peroxide. In addition, the enzyme catalyzes the twoelectron reduction of 1,4-benzoquinone, several substituted benzoquinones, and 2,6-dichloroindophenol, as well as the one-electron reduction of the ABTS [2,2-azinobis(3-ethylbenzthiazolinesulfonic acid)] cation radical. As judged by the catalytic efficiencies (k cat /K m ), some of these quinone electron acceptors are much better substrates for pyranose oxidase than oxygen. The optimum pH of the pyranose oxidase-catalyzed reaction depends strongly on the electron acceptor employed and varies from 4 to 8. It has been proposed that the main metabolic function of pyranose oxidase is as a constituent of the ligninolytic system of white rot fungi that provides peroxidases with H 2 O 2 . An additional function could be reduction of quinones, key intermediates that are formed during mineralization of lignin.The enzyme pyranose oxidase (P2O) (pyranose:oxygen 2-oxidoreductase; EC 1.1.3.10), which catalyzes the oxidation of several aldopyranoses at position C-2 to yield the corresponding 2-ketoaldoses (aldos-2-uloses, osones), is widely distributed among wood-degrading basidiomycetes (14,32,44). It has been purified and characterized from several microorganisms, including Phanerochaete chrysosporium (2, 45), Phlebiopsis gigantea (39), Pleurotus ostreatus (40), Polyporus obtusus (28), Trametes (Coriolus) versicolor (35), and unidentified basidiomycete no. 52 (26). The currently available data reveal some general similarities among P2Os from these different fungi. Typically, P2O is a rather large, homotetrameric protein that contains covalently bound flavin adenine dinucleotide (FAD). The in vivo substrates of P2O probably are D-glucose, D-galactose, and D-xylose, which are abundant in lignocellulose and which are oxidized to 2-keto-D-glucose (D-arabino-hexos-2-ulose, 2-dehydro-D-glucose), 2-keto-D-galactose (D-lyxo-hexos-2-ulose, 2-dehydro-D-galactose), and 2-keto-D-xylose (D-threopentos-2-ulose, 2-dehydro-D-xylose), respectively. In addition, P2O also exhibits significant activity with a number of other carbohydrates, including L-sorbose, D-glucono-1,5-lactone, and D-allose (20). The substrate selectivity, however, varies to some extent among P2Os isolated from different fungi. During the oxi...

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Purification and Characterization of Pyranose Oxidase from the White Rot Fungus Trametes multicolor

Leitner¹,

Volc

Haltrich³

2001

Appl Environ Microbiol

Self Cite

146

166

View full text Add to dashboard Cite

show abstract

“…Remarkably, the dicarbonyl sugar derivatives are gaining an increased importance as intermediates in sugar transformations, i.e. aldose→ke-tose, relevant for food biotechnology (Freimund et al 1996(Freimund et al , 1998Leitner et al 1998).…”

Section: Introductionmentioning

confidence: 99%

Screening of basidiomycete fungi for the quinone-dependent sugar C-2/C-3 oxidoreductase, pyranose dehydrogenase, and properties of the enzyme from Macrolepiota rhacodes

Volc

Kubátová

Daniel

et al. 2001

Archives of Microbiology

Self Cite

View full text Add to dashboard Cite

Mycelial cultures of 76 strains of lignocellulose-degrading basidiomycete fungi were screened for the activity of pyranose dehydrogenase, a novel sugar oxidoreductase recently detected in Agaricus bisporus. Of these fungi, 37 strains belonging to seven phylogenetically related genera of mostly litter-decomposing Agaricales were positive for the dehydrogenase, based on activity assays towards D-glucose with 1,4-benzoquinone or ferricenium ion as electron acceptors, and on TLC/HPLC analyses of the reaction products. Lack of activity with O(2) as the oxidant, specificity for C-3 of D-glucose, and active extracellular secretion of the enzyme were used as criteria to differentiate pyranose dehydrogenase from pyranose 2-oxidase (EC 1.1.3.10), known to be produced by numerous wood-rotting fungi. Extracellular pyranose dehydrogenase from Macrolepiota rhacodes was heavily glycosylated. The enzyme was characterized as a 78-kDa flavoprotein under denaturing conditions and a 76-kDa native protein using gel filtration. This enzyme had a maximum extracellular activity of 4.1 U ml(-1) in 39-day liquid cultures. It exhibited broad selectivity for sugar substrates and oxidized D-glucose (K(m)=1.82) exclusively at C-3 to 3-dehydro-D-glucose (D-ribo-hexos-3-ulose), in contrast to pyranose dehydrogenases from Agaricus species, which acted at both C-3 and C-2 of D-glucose. The N-terminal sequence, AVVYRHPDEL, showed significant similarity with that reported for A. bisporus.

show abstract

“…This rather low degree of bioconversion for the biomass compared with the cell-free extract may be due to mass transfer limitations (Fig. 5c), which has been reported by several researchers [25,26]. The presence of catalase in the reaction mixture was also investigated on the degree of conversion as shown in Fig.…”

Section: Biocatalysis At Moderate Pressures and Atmospheric Pressure mentioning

confidence: 95%

Bioconversion of d-glucose into d-glucosone by Glucose 2-oxidase from Coriolus versicolor at Moderate Pressures

Karmali

Coelho

2010

Appl Biochem Biotechnol

View full text Add to dashboard Cite

Abstract:The immobilized glucose 2-oxidase (pyranose oxidase, pyranose:oxygen-2-oxidoreductase, EC 1.1.3.10) from Coriolus versicolor was used to convert D-glucose into D-glucosone at moderate pressures, up to 150 bar, with compressed air in a modified commercial batch reactor. Several parameters affecting biocatalysis at moderate pressures were investigated as follows: pressure, different forms of immobilized biocatalysts, glucose concentration, pH, temperature and the presence of catalase. Glucose 2-oxidase (GOX2) was purified by immobilized metal affinity chromatography on epoxy-activated Sepharose 6B-IDA-Cu(II) column at pH 6.0. Purified enzyme and catalase were immobilized into a polyethersulfone (PES) membrane in the presence of glutaraldehyde and gelatin. Enhancement of the bioconversion of D-glucose was done by the pressure since an increase in the pressure with compressed air increases the conversion rates. The optimum temperature and pH for bioconversion of D-glucose were found to be 62 degrees C and pH 6.0, respectively and the activation energy (E(a)) was 28.01 kJ mol(-1). The apparent kinetic constants (V(max)' K(m)', K(cat)' and K(cat)/K(m)') for this bioconversion were 2.27 U mg(-1) protein, 11.15 mM, 8.33 s(-1) and 747.38 s(-1) M(-1), respectively. The immobilized biomass of C. versicolor as well as crude extract containing GOX2 activity were also useful for bioconversion of D-glucose at 65 bar with a yield of 69.9 +/-3.8% and 91.3 +/-1.2%, respectively. The immobilized enzyme was apparently stable for several months without any significant loss of enzyme activity. On the other hand, this immobilized enzyme was also stable at moderate pressures, since such pressures did not affect significantly the enzyme activity. (C)

show abstract

The Cetus Process Revisited: A Novel Enzymatic Alternative for the Production of Aldose-Free D-Fructose

Cited by 49 publications

References 35 publications

Purification and Characterization of Pyranose Oxidase from the White Rot Fungus Trametes multicolor

Purification and Characterization of Pyranose Oxidase from the White Rot Fungus Trametes multicolor

Screening of basidiomycete fungi for the quinone-dependent sugar C-2/C-3 oxidoreductase, pyranose dehydrogenase, and properties of the enzyme from Macrolepiota rhacodes

Bioconversion of d-glucose into d-glucosone by Glucose 2-oxidase from Coriolus versicolor at Moderate Pressures

Contact Info

Product

Resources

About