University of North Florida
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Contact Info

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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Carl-Fredrik Mandenius

Abbrev:
Mandenius, C.F.
Other Names:
Address:
Division of Biotechnology, Department of Physics and Measurement Technology, Linköping University, 58183 Linköping, Sweden
Phone:
+46-13-288967
Fax:
+46-13-288969

Citations 5

"Growth Behavior In Plant Cell Cultures Based On Emissions Detected By A Multisensor Array"
Biotechnol. Prog. 2004 Volume 20, Issue 4 Pages 1245-1250
Palle Komaraiah, Marian Navratil, Maria Carlsson, Paul Jeffers, Maria Brodelius, Peter E. Brodelius, Patricia M. Kieran and Carl-Fredrik Mandenius

Abstract: The use of a multisensor array based on chemical gas sensors to monitor plant cell cultures is described. The multisensor array, also referred to as an electronic nose, consisted of 19 different metal oxide semiconductor sensors and one carbon dioxide sensor. The device was used to continuously monitor the off-gas from two plant cell suspension cultures, Morinda citrifolia and Nicotiana tabacum, cultivated under batch conditions. By analyzing the multiarray responses using two pattern recognition methods, principal component analysis and artificial neural networks, it was possible to monitor the course of the cultivations and, in turn, to predict (1) the biomass concentration in both systems and (2) the formation of the secondary metabolite, antraquinone, by M. citrifolia. The results identify the multisensor array method as a potentially useful analytical tool for monitoring plant process variables that are otherwise difficult to analyze on-line.

"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.
Monosaccharides Glucose Galactose Xylose Amperometry Immobilized enzyme Controlled pore glass Interface Dialysis Membrane Enzyme

"Quantitation Of Intracellular Recombinant Human Superoxide Dismutase Using Surface Plasmon Resonance"
Anal. Chim. Acta 2002 Volume 456, Issue 2 Pages 193-200
Daniel Ivansson, Karl Bayer and Carl-Fredrik Mandenius

Abstract: An immunosensor assay for the quantitation of intracellular recombinant human superoxide dismutase (rhSOD) in Escherichia coli cultivations based on detection with surface plasmon resoance (SPR) is described. A monoclonal antibody for rhSOD was immobilized on a SPR dextran gold chip. Bacterial samples were sonicated and centrifugated prior to injection over the antibody chip for SPR detection. The assay time was 7 min and allowed quantitation in the range of 1-64 nM SOD in lysate samples with a precision of 1.1-3.4%. The assay was applied to monitor the concentration of rhSOD during E. coli bioreactor cultivations where the rhSOD production was induced by iso-propyl-b-D-thiogalactoside (IPTG). The assay allowed accurate monitoring of the production of rhSOD where the important phases in the product formation were possible to see. The report also discusses influence from sample preparation, SPR selectivity and sensitivity and quantitation limits. The assay proved to be fast, sensitive and accurate with low background effects from the dextran matrix of the SPR chip.
Optimization

"In-situ Ethanol Probe Based On Sample Dilution In A Double Membrane System"
Anal. Chim. Acta 1988 Volume 215, Issue 1 Pages 71-77
Carl Fredrik Mandenius

Abstract: An in-situ probe suitable for monitoring ethanol in fermenters or other bioreactors is described. It is constructed with an ethanol-permeable double membrane covering a solid-state tin(IV) oxide sensor for gas detection. A stream of nitrogen is passed between the two membranes in order to dilute the ethanol vapor from the fermenter that has passed through the first membrane, before it reaches the second membrane covering the detector. A 100-fold dilution was obtained at a flow rate of 30 mL min-1 of the diluent gas. The delay time was less than 5 min to obtain 80% of maximum response.
Ethanol Fermentation broth Biotechnology Conductometry Electrode Dilution Gas diffusion Membrane

"Monitoring And Control Of Enzymic Sucrose Hydrolysis Using On-line Biosensors"
Appl. Microbiol. Biotechnol. 1985 Volume 21, Issue 3-4 Pages 135-142
C. F. Mandenius , L. Bülow, B. Danielsson and K. Mosbach

Abstract: Previously reported flow microcalorimeter devices for enzymatic reaction heat measurement, enzyme thermistors, have here been extended with systems for on-line sample treatment. Glucose analysis was performed by intermittent flow injections of 50 µL samples through such an enzyme thermistor device containing immobilized glucose oxidase and catalase. Sucroce analysis was performed by allowing diluted samples to continuously pass through an additional enzyme thermistor containing immobilized invertase. The reaction heats were recorded as temperature changes in the order of 10^-50 m°C for concentrations of 0.05-0.30 M glucose or sucrose present in the original non-diluted samples. The performance of this system was investigated by its ability to follow concentration changes obtained from a gradient mixer. The system was applied to monitoring and controlling the hydrolysis of sucrose to glucose and fructose in a plug-flow reactor with immobilized invertase. The reactor was continuously fed by a flow of scurose of up to 0.3 M (100 g/l). Glucose and remaining sucrose were monitored in the effluent of the column. By using flow rate controlled feed pumps for sucrose and diluent the influent concentration of sucrose was varied while the overall flow rate remained constant.