University of North Florida
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Stuart Chalk, Ph.D.
Department of Chemistry
University of North Florida
Phone: 1-904-620-1938
Fax: 1-904-620-3535
Email: schalk@unf.edu
Website: @unf

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Xylose

  • IUPAC Name: (3R,4S,5R)-oxane-2,3,4,5-tetrol
  • Molecular Formula: C5H10O5
  • CAS Registry Number: 25990-60-7
  • InChI: InChI=1S/C5H10O5/c6-1-3(8)5(10)4(9)2-7/h1,3-5,7-10H,2H2/t3-,4+,5+/m0/s1
  • InChI Key: SRBFZHDQGSBBOR-IOVATXLUSA-N

@ ChemSpider@ NIST@ PubChem

Citations 9

"Flow Injection System For The Amperometric Determination Of Xylose And Xylulose With Co-immobilized Enzymes And A Modified Electrode"
Anal. Chim. Acta 1988 Volume 213, Issue 1-2 Pages 139-150
E. Dominguez and B. Hahn-Hägerdal, G. Marko-Varga and L. Gorton

Abstract: A purpose-built flow injection analysis system was constructed that incorporated a 25 µL reactor containing xylose isomerase (omitted in determination of xylose alone), aldose 1-epimerase and glucose dehydrogenase immobilized on CPG-10 glass beads (37 to 74 µm diameter; 51.5 nm pore size). The NADH produced from NAD+ incorporated in the carrier solution [0.1 M phosphate buffer (pH 7.0) containing Mg] was detected electrochemically with use of a dye-modified graphite electrode in a wall-jet configuration (cf. Appleqvist et al., Anal. Abstr., 1985, 47, 12D151). Up to 30 determinations per hour were possible and calibration graphs were rectilinear for up to 2 mM xylose or -xylulose.
Feed Industrial Amperometry Electrode Sample preparation Controlled pore glass Extraction Immobilized enzyme

"Determination Of Xylose And Glucose In A Flow Injection System With PQQ [pyrroloquinoline Quinone-]dependent Aldose Dehydrogenase"
Anal. Chim. Acta 1993 Volume 280, Issue 1 Pages 119-127
Maria Smolander*, Julia Cooper, Wolfgang Schuhmann, Martin Hämmerle and Hanns-Ludwig Schmidt

Abstract: PQQ-dependent aldose dehydrogenase was immobilized on (i) glutaraldehyde-activated controlled-pore glass (1400 .angstrom.), (ii) a heat-treated carbodi-imide-activated graphite electrode or (iii) an Os-containing redox polymer. Different flow injection systems were investigated to optimize the measurements; the highest current densities were obtained with (ii) and the best stability with (i). For the analysis of fermentation samples containing xylose as the only C source the (i) system was used, with 500 µm-phenazine methosulfate added as a mediator in a carrier stream of 50 mM potassium phosphate of pH 6.5. Results for xylose agreed well with those obtained by HPLC. For samples containing both xylose and glucose, the glucose was determined separately by incorporating a glucose oxidase column in the flow system, by use of a test kit or by HPLC; the xylose concentration. could then be calculated by compensating for the effect of glucose on the xylose calibration graph.
HPLC Immobilized enzyme Controlled pore glass

"Aldose Dehydrogenase-modified Carbon Paste Electrodes As Amperometric Aldose Sensors"
Anal. Chim. Acta 1995 Volume 302, Issue 2-3 Pages 233-240
Maria Smolander*, György Marko-Varga and Lo Gorton

Abstract: A solution of aldose 1-dehydrogenase in 10 mM sodium acetate of pH 5 containing 0.1% of Triton X-100 was applied to the polished tip (diameter 1.7 mm) of a carbon paste electrode; results were less satisfactory when the enzyme was first mixed with the carbon paste. Incorporation of 2% (relative to graphite) of dimethylferrocene in the paste led to high catalytic response. The prepared electrode was coated with Eastman AQ-29D from aqueous 0.5% solution; this improved stability and minimized non-specific responses. Amperometric measurements with the electrode were made at +200 mV vs. Ag/AgCl (Pt counter electrode) in a flow injection system with 50 mM sodium phosphate buffer of pH 6.5 as carrier at 0.7 ml/min. Solutions of glucose and xylose standards and aldose samples were prepared in the same buffer. Xylose from a yeast fermenter was separated by LC on an Aminex HPX-87P column (30 cm x 7.8 mm i.d.) in Pb(II) form. The enzyme was active mainly towards the β-anomer of glucose. Response was linear up to 100 mM xylose and 10 mM glucose.
Fermentation broth Sensor Amperometry Electrode Electrode Apparatus Triton X Surfactant

"Determination Of Monosaccharides In Cellulosic Hydrolysates Using Immobilized Pyranose Oxidase In A Continuous Amperometric Analyser"
Anal. Chem. 1990 Volume 62, Issue 24 Pages 2688-2691
Lisbeth Olsson, Carl Fredrik Mandenius, and Jindrich Volc

Abstract: Purified pyranose oxidase (details given) was immobilized on controlled pore glass by using the glutaraldehyde activation method and stabilized by co-immobilization with catalase. For the determination of glucose, xylose and galactose, the immobilized enzyme reactor was installed in a pseudo flow injection system and oxygen consumption was measured with an amperometric electrode (Clark-type). The electrode response after partial transfer of the sample through a dialysis membrane was rectilinear from 0.6 to 30, 1.0 to 50 and 2.0 to 100 mM, respectively. The analytical system was tested for bioreactor monitoring on laboratory scale by interfacing with a 10-l fermenter containing spent sulfite liquor, and no adverse effects were observed with regard to pyranose response; after 2000 injections into the enzyme reactor the decay of enzyme activity was 17%. This analytical system has also been applied to the continuous monitoring of ethanolic fermentation.
Amperometry Immobilized enzyme Controlled pore glass Interface Dialysis Membrane Enzyme

"Postchromatographic Electrochemical Detection Of Carbohydrates At A Silver Oxide Electrode"
Electroanalysis 1993 Volume 5, Issue 8 Pages 669-675
Terrence P. Tougas, Mark J. Debenedetto, James M. Demott Jr.

Abstract: An oxide surface was formed on a 2-mm Ag-wire electrode by conditioning in 0.1 M NaOH at +0.7 V for 30 min and then at 0.45 V vs. the SCE. The properties of the electrode were studied and it was applied to the electrochemical detection of simple sugars separated by HPLC on a Waters carbohydrate analysis column (30 cm x 3.9 mm) with mobile phase (1 ml/min) of acetonitrile/phosphate buffer of pH 8 (36:11) and by FIA. Calibration graphs were rectilinear for 1-100 µM-galactose, glucose, ribose and xylose.
Electrode Electrochemical analysis HPLC Post-column derivatization

"Ferrocene-containing Polymers As Electron Transfer Mediators In Carbon Paste Electrodes Modified With PQQ-dependent Aldose Dehydrogenase"
Electroanalysis 1995 Volume 7, Issue 10 Pages 941-946
Maria Smolander, Lo Gorton, Hung Sui Lee, Terje Skotheim, Hsing-Lin Lan

Abstract: Four different polymer-bound ferrocene derivatives were evaluated as electron transfer mediators in aldose biosensors based on aldose dehydrogenase with pyrroloquinoline quinone (PQQ) as co-enzyme. The polymeric ferrocene derivatives (syntheses described) were mixed with C paste and packed into a plastic syringe holder that had been pre-packed with unmodified C paste. A solution of aldose dehydrogenase in 10 mM sodium acetate of pH 5 containing 0.1% Triton X-100 was applied to the electrode surface and allowed to dry. The electrodes were evaluated in a flow injection system equipped with a wall-jet amperometric cell using 50 mM sodium phosphate buffer of pH 6.5 as carrier (0.7 ml/min). Maximum response was obtained at +300 mV vs. Ag/AgCl but measurements were normally made at +200 mV to minimize interference from non-specific oxidation processes. The electrodes were more stable than those modified with monomeric dimethylferrocene. The best response was obtained with polymethyl(11-ferrocenyl-4,7,10-trioxa-undecanyl)methyl (12-amino-4,7,10-tioxa-dodecyl)siloxane (1:1) and electrodes prepared from this derivative was applied to the determination of xylose in fermentation mixtures; the results agreed with those obtained by LC.
Fermentation broth Sensor Electrode Electrode Amperometry Electrode Interferences Method comparison Triton X Surfactant

"Analysis Of Pentoses In Dry Wine By High Performance Liquid Chromatography With Post-column Derivatization"
Am. J. Enol. Vitic. 1986 Volume 37, Issue 4 Pages 269-274
Bruce D. Franta, Leonard R. Mattick, and John W. Sherbon

Abstract: Wine samples were adjusted to pH 8 to 9 with concentrated aqueous NH3 and diluted with water before separation of the pentoses on an HPX-87P lead cation-exchange column (30 cm x 7.8 mm), at 70°C, fitted with an Aminex HPX-87C carbohydrate pre-column. Post-column derivatization with tetrazolium blue(I) was achieved with a reagent solution containing 80% ethanol - 0.01 M NaOH - 0.1% I at 1.1 mL min-1 and a 1.8-m reaction coil at 85°; detection was at 520 nm. The rectilinear ranges for xylose, arabinose, ribose, glucose and rhamnose extended up to 2.4 µg (that for fructose up to 1.2 µg), coefficient of variation were ~2% and detection limits were <0.3 µg. The method was only applicable to dry wines as large glucose concentration. (e.g., in sweet wines) affected the determination of xylose.
Wine HPLC Spectrophotometry Heated reaction Post-column derivatization

"Flow Stream Detectors Based On Electrocatalytic Oxidation Of Polyhydroxy Compounds At Silver Oxide Electrodes"
Contemp. Electroanal. Chem. 1990 Volume 1, Issue 1 Pages 275-296
Terrence P. Tougas, Edwin G. E. Jahngen, Michael Swartz

Abstract: Many simple carbohydrates and other polyhydroxy compounds can be oxidized at a silver oxide surface. The oxidation is via an electrocatalytic mechanism involving a Ag(I) oxide. This forms the basis of a flow stream detector operated in an amperometric mode which may be used for either flow injection or high performance liquid chromatography (HPLC) applications. The title electrode has been applied to the detection of simple carbohydrates, triglycerides and nucleic acid components.
Electrode Amperometry Detector

"Analysis Of Various Sugars By Means Of Immobilized Enzyme Coupled Flow Injection Analysis"
J. Biotechnol. 1996 Volume 50, Issue 2-3 Pages 93-106
B. Weigela, B Hitzmanna, G. Kretzmera, K. Sch&uuml;gerla,*, A. Huwigb and F. Giffhornb

Abstract: Glucose, maltose, sucrose, lactose, xylose, sorbose, galactose, fructose and gluconolactone were analyzed by means of immobilized pyranose oxidase as well as by the combination of immobilized glucose oxidase with immobilized glycoamylase, invertase, mutarotase, maltase (α-glucosidase) and glucose isomerase by flow injection analysis (FIA). For the simultaneous analysis of glucose and other sugars three different flow injection configurations were applied and compared. The average error of prediction of the analyzes were better than 3% in model media and better than 6% in yeast extract containing media.
Chemiluminescence Immobilized enzyme Simultaneous analysis Manifold comparison