Laboratory procedures for producing 2-keto-d-glucose, 2-keto-d-xylose and 5-keto-d-fructose from d-glucose, d-xylose and l-sorbose with immobilized pyranose oxidase of Peniophora gigantea

Huwig, Alexander; Danneel, Hans-Jürgen; Giffhorn, Friedrich

doi:10.1016/0168-1656(94)90217-8

Cited by 55 publications

(32 citation statements)

References 16 publications

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“…Evidence for the bicyclic double acetal structure of 42 and 43 was given by the chemical shifts for the C-2 carbons at 101 ± 103 ppm in addition to the downfield shifts for C-5, as well as the very profound sensitivity of the C-6 resonances for the anomeric configuration. The 1 H NMR coupling data and chemical shifts are in agreement with bicyclic structures that have previously been described for ketoaldoses, [28,29] 2-keto-glycopyranosides, [30] aqueous solutions of d-allosone (15) and 3-deoxy-glucosone (18) and in organic solutions of d-glucosone (2). [27] Hydrogenation of d-allosone (15) with Pd/C afforded a mixture of d-psicose, [27] d-allose and d-altrose [31,32] in a ratio of 5:4:1 according to 1 H NMR spectroscopy (Table 3).…”

Section: Resultssupporting

confidence: 78%

“…Dicarbonyl sugars are, for example, found in mammalian tissues, in which they are involved in the cross-linking of proteins and thus affect tissue functions. d-Glucosone (2) is assumed to be formed by autooxidation of glucose [9] or other processes in mammals, [10] and the biochemically most important 3-deoxy-d-glucosone (18) occurs in blood and urine [11] in concentrations that are elevated in diabetes. [12] 1,5-Anhydro-d-fructose (20) is believed to be a metabolite of 1,5-anhydro-d-glucitol (12), which is present in cerebrospinal fluids and plasma, and plays a role in diabetes.…”

Section: Introductionmentioning

confidence: 99%

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Rare Keto-Aldoses from Enzymatic Oxidation: Substrates and Oxidation Products of Pyranose 2-Oxidase

Freimund¹,

et al. 1998

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Pyranose oxidases are known to oxidise d-glucose, d-xylose and lsorbose to keto-aldoses, biochemically interesting compounds that may also be used for synthetic purposes in a variety of reactions. In this study pyranose oxidase from the basidiomycete Peniophora gigantea was investigated, and it was found that this enzyme is able to oxidise a broad variety of substrates very effectively. In analogy to its natural mode of action, most substrates are oxidised regioselectively in position 2. Certain compounds, however, are converted into 3-keto derivatives, and the enzyme even exhibits transfer potential, that is, disaccharides are formed from bglycosides of higher alcohols. Substrates that may be oxidised at C-2 in yields between 40 ± 98 % are d-allose, d-galactose, 6-deoxy-d-glucose, d-gentiobiose, a-d-glucopyranosyl fluoride and the very interesting 3-deoxy-d-glucose. 1,5-Anhydro-d-glucitol (1-deoxy-d-glucose) is very effectively oxidised in position 2 in 98 % yield and additionally gives a product of dioxidation at C-2 and C-3 upon prolonged reaction time. Selective oxidation at C-3 was found for 2-deoxyd-glucose in very good yields and for methyl b-d-gluco-and methyl b-galactopyranoside in lower yields. All oxidation products were unequivocally characterised by NMR spectroscopy and/or chemical derivatisation. In addition, the kinetic data of the enzymatic reactions were determined for all substrates. On the basis of these data and the structural characteristics of the substrates, a model for the minimal structural requirements of the enzyme ± substrate interaction is suggested. The enzyme presumably uses two different binding modes for the regioselective C-2 and the C-3 oxidations, which are described.

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Section: Resultssupporting

confidence: 78%

Section: Introductionmentioning

confidence: 99%

Rare Keto-Aldoses from Enzymatic Oxidation: Substrates and Oxidation Products of Pyranose 2-Oxidase

Freimund¹,

et al. 1998

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“…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%

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

Leitner¹,

Volc

Haltrich³

2001

Appl Environ Microbiol

146

166

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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...

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“…Prior to analysis proteins were removed by heat treatment and centrifugation. A Benson-100 carbohydrate column (Benson Polymeric Inc., Reno, Nev.) linked with a refractive index detector (model 156; Beckman, Frankfurt, Germany) was used, and water was the mobile phase at a column temperature of 85°C and a flow rate of 0.85 ml/min (17).…”

Section: Methodsmentioning

confidence: 99%

“…TLC was performed on silica gel plates (Merck, Darmstadt, Germany) using acetone-butanol-water (4:5:1) as the mobile phase. Spots were detected with dinitrophenylhydrazine reagent (17).…”

Section: Methodsmentioning

confidence: 99%

l-Glucitol Catabolism inStenotrophomonas maltophiliaAc

Brechtel

Huwig

Giffhorn

2002

Appl Environ Microbiol

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Laboratory procedures for producing 2-keto-d-glucose, 2-keto-d-xylose and 5-keto-d-fructose from d-glucose, d-xylose and l-sorbose with immobilized pyranose oxidase of Peniophora gigantea

Cited by 55 publications

References 16 publications

Rare Keto-Aldoses from Enzymatic Oxidation: Substrates and Oxidation Products of Pyranose 2-Oxidase

Rare Keto-Aldoses from Enzymatic Oxidation: Substrates and Oxidation Products of Pyranose 2-Oxidase

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

l-Glucitol Catabolism inStenotrophomonas maltophiliaAc

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