Skip to main content
SpringerLink
Log in

Film-Forming Aminocellulose Derivatives as Enzyme-Compatible Support Matrices for Biosensor Developments

  • Published:
Cellulose Aims and scope Submit manuscript

Abstract

Based on 6(2)-O-tosyl celluloses and 6(2)-O-tosylcellulose derivatives, it has been possible to synthesize a novel soluble aminocellulose type, P-CH2-NH-(X)-NH2 (P=cellulose, (X)=alkylene, aryl, aralkylene or oligoamine) with diamine or oligoamine residues at C6 and solubilizing groups (S) such as acetate, benzoate, carbanilate, methoxy and/or tosylate groups at C2/C3 of the anhydroglucose unit (AGU). Depending on the nature and degree of substitution (DS) of (S), the aminocelluloses are soluble either in DMA and DMSO or in water. They all form transparent films from their solutions. In the case of water-soluble aminocelluloses, for example, an enzyme-specific pH value can be adjusted by protonation of the NH2 end groups at C6. The aminocelluloses apparently form aggregates (on a scale of nanostructures) according to a structure-inherent organization principle. The nanostructures could be imaged on the aminocellulose film surface by atomic force microscopy (AFM) in the form of characteristic topographic structures – as a result of the aggregation of the aminocellulose derivative chains and their interaction with the functionalized film support. In this way, structural and environment-induced factors influencing the nanostructure formation were found. The aminocellulose films can be covalently coupled with biomolecules by bifunctional reaction via NH2-reactive compounds. With the aid of analytically relevant enzymes, e.g. glucose oxidase (GOD), horseradish peroxidase (HRP) and others, it was found that the enzyme parameters can be modified by the interplay of the aminocellulose and coupling structures. A number of new bifunctional enzyme coupling reactions, e.g. via L-ascorbic acid or benzenedisulfonyl chlorides, forming amide or sulfonamide coupling structures led to efficient enzyme activities and long-term stabilities in the case of GOD and HRP coupling to PDA cellulosetosylate films.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  • Alvarez-Tcaza M., Kalisz H. M., Hecht H. J., Aumann K.-D., Schomburg D. and Sclimid R. D. 1995. The design of enzyme sensors based on the enzyme stricture. Biosens. Bioelectr. 10: 735–742.

    Google Scholar 

  • Arica MY. and Hasirci V. 1993. Glucose oxidase sandwiched between pHEMA layers: a continuous flow reactor application. Biomaterials 14: 809–816.

    PubMed  Google Scholar 

  • Baimin A. V., Eremenko A. V., Sokolovslcij A. A., Chemov S. F. and Kurochkin TN. 1993. New catalytic properties of glucose oxi-dase in monomolecular films. Biotecimol. Appl. Biochem. 18: 369–376.

    Google Scholar 

  • Barthel H., Rosch L. and Weis J. 1996. Fumed silica production, properties and applications. In: Auner M. and Weis J. (eds), Organo Silicon Chemistry II-From Molecules to Materials. VCllVerlagsgesellschaft mbll, Weinheim, Geimany, pp. 76 ff.

    Google Scholar 

  • Becher J., Liebegott H., Berlin P. and Klemm D. 2003. Novel xylylene di-aminocellulose derivatives for enzyme immobiliza-tion. Cellulose (accepted for publication).

  • Berlin P., Tiller J., Rieseler R. and Klemm D. 1998. Supramolekulare Erkeimungsstnikturen auf Cellulosebasis. Das Papier 52: 737–742.

    Google Scholar 

  • Berlin P., Klemm D., Tiller J. and Rieseler R. 2000. Feature-A novel soluble aminocellulose derivative type: its transparent film-forming properties and its efficient coupling with enzyme proteins for biosensors. Macromol. Chem. Phys. 201: 2070–2082.

    Google Scholar 

  • Berlin P., Tiller J. and Klemm D. 1997a. New aromatic amino-cellulose derivatives and process for their preparation. Patent EP 0 873 365 B1 (WO 97/25353), Forschungszentrum Jiilich GmbH. Chem. Abstr. 1997, 127, 150–332.

    Google Scholar 

  • Berlin P., Tffler J. and Klemm D. 1997a. New (bio)chemical reagent solid phases, process for their production and their applications. Patent EP 0 883 812 B1 (WO 97/25621), Forschungszentrum Jiilich GmbH. Chem. Abstr. 1997, 127, 133103.

  • Berlin P., Tifier J. and Klemm D. 2002. (Bio)chemical reagent solid phases, process for their production and their applications. US Patent 6, 358, 754 B1, Forschungszentnim Jiilich GmbH.

  • Bisswanger H. 1994. Enzymkinetik-Theorie mid Methoden. VCH Verlagsgemeinschaft mbll, Weinheim, Geimany.

    Google Scholar 

  • Braun D. and Meuret B. 1989. Benzyl-cellulose as thermoplastic synthetic substance. 1. Preparation and characterization. Das Papier 43: 688–693.

    Google Scholar 

  • Chang H. Y. and Bae Z.-U. 1997. Adenosine-modified electrodes for the determination of glucose without using an immobilized redox mediator. Anal. Lett. 30: 1981–1992.

    Google Scholar 

  • Chibatu I. 1978. Preparation of immobilized enzymes and microbial cells. Main entry under title: Immobilized enzymes, research and development. Kodanska Scientific Books, Tokyo, Japan and Halsted Press, New York.

    Google Scholar 

  • Comfort A. R., Albeit E. and Langer R. 1989a. Immobilized enzyme cellulose hollow fibers: immobilization of heparinase. Biotecimol. Bioeng. 34: 1366–1374.

    Google Scholar 

  • Comfoit A. R., Albeit E. and Langer R. 1989b. Immobilizedenzyme cellulose hollow fibers: II. kinetic analysis. Biotechnol. Bioeng. 34: 1374–1382.

    Google Scholar 

  • Corbett J. F. 1973. Role of m-difunctional benzene derivatives in oxidative hair dyeing. I. Reaction ith p-diamines. J. Soc. Cosmet. Chem. 24: 103–134.

    Google Scholar 

  • Dade J. V., Revol J.-F., Gail F. and Coffinet G. 1992. Characterization and supramolecular architecture of the cellu-lose-protein in the tunic of sea perch. Biol. Cell. 76: 87–96.

    Google Scholar 

  • Daly W. H. and Lee S. 1989. Peptide graft-copolymers from soluble 6-aminodeoxycellulose acetate. Abstr. Pap. Am. Chem. 5. 198: 52-Poly. September 10.

  • Daly W. H. and Munir A. 1984. Aminopropylcellulose, synthesis and derivatization. J. Polym. Sci. Pol. Chem. 22: 975–984.

    Google Scholar 

  • Enmeus J. and Gorton L. 1993. Comparison between different inorganic supports for the immobilization of amyloglucosidase and alpha-amylase to be used in enzyme reactors in flow-injection systems. 2. Hydrolysis of glycogen. Anal. Chim. Acta 276: 319–328.

    Google Scholar 

  • Englebretsen D. R. and Harding D. R. K. 1992. Solid-phase peptide-synthesis on hydrophilic supports. 2. Studies using perloza beaded cellulose. Int. J. Protein Res. 40: 487–496.

    Google Scholar 

  • Englebretsen D. R. and Harding D. R. K. 1994. High-yield, directed immobilization of a peptide ligand onto a beaded cellulose sup-port. Pept. Res. 7: 322–326.

    PubMed  Google Scholar 

  • Entcheva E. G. and Yotova L. K. 1994. Analytical application of membranes with covalently bound glucose oxidase. Anal. Chim. Acta 299: 171–177.

    Google Scholar 

  • Erler U., Misclinick P., Stein A. and Klemm D. 1992. Deteimination of the substituent patterns of cellulose methyl ethers by HPLC and GLC-comparison of methods. Polymer Bull. 29: 349–356.

    Google Scholar 

  • Frew J. E. and Hill H. A. 0. 1987a. Electrochemical biosensors. Anal. Chem. 59: A933.

    Google Scholar 

  • Frew J. E. and Hill H. A. 0. 1987b. Electron-transfer biosensors. Phil. Trans. R. Soc. London B 316: 95–106.

    Google Scholar 

  • Fultz M. L. and Durst R. A. 1982. Mediator compounds for the electrochemical study of biological redox systems: a compila-tion. Anal. Chim. Acta 140: 1–18.

    Google Scholar 

  • Gavlik J. and Tokar 0. 1989. CS 259 795. Chem. Abstr. 1990, 113, 8291.

  • Gemeiner P. 1982. Aldehydic derivatives of bead cellulose-relationships between the matrix structure and function in immobilization of enzyme catalyzing hydrolysis of high mole-cular substrates. Biotecimol. Bioeng. 24: 2573–2582.

    Google Scholar 

  • Göpel W., Jones T. A., Kleitz M., Lundström J. and Seiyame T. 1992. Chemical and biochemical sensors, part II. In: Göpel W., Hesse J. and Zemel J. N. (eds.), Sensors-A CompreheisiveSurvey, Vol. 3. VCllVerlagsgesellschaft mbH, Weinheim, Geimany.

    Google Scholar 

  • Göpel W. and Ziegler Ch. 1992. Nanostructures Based on Molecular Materials, Molecular Electronic – Part I: Design of Molecular Functional Units. VCH Verlagsgesellschaft mbH, Weinheim, Geimany, pp. 9–75.

    Google Scholar 

  • Göpel W. 1994. New materials and transducers for chemical sen-sors. Sensors Actuators B 18–19: 1–21.

    Google Scholar 

  • Golub A. A., Zubenko Ad. and Zlimud B. V. 1996. 7-APTES mod-ified silica gels: the structure of the surface layer. J. Coll. Interface Sci. 179: 482–487.

    Google Scholar 

  • Gomez J. A. C., Erler U. and Klemm D. 1996. 4-Methoxy-substituted trityl groups in 6–0-protection of cellulose: Homogeneous synth-esis, characterization, detritylation. Macromol. Chem. Phys. 197: 953–964.

    Google Scholar 

  • Goncalves A. P. A., Martins M. B. F. and Cniz M. E. M. 1991. Analytical use of immobilized glucose oxidase-kinetic and operational studies. Appl. Biochem. Biotechnol. 27: 139–143.

    Google Scholar 

  • Gregg B. A. and Heller A. J. 1991. Redox polymer-films contairing enzymes. 2. Glucose-oxidase containing enzyme electrodes. J. Phys. Chem. 95: 5976–5980.

    Google Scholar 

  • Greenfield P. F., Kittrell J. R. and Laurence R. L. 1975. Inactivation of immobilized glucose oxidase by hydrogen peroxide. Anal. Biochem. 65: 109–124.

    PubMed  Google Scholar 

  • Guilbault G. G. and de Olivera N. G. 1985. Immobilisation enzyme electrodes. In: Woodward J. (ed), Immobilised Cells and Enzymes-A Practical Approach. IRL Press Ltd., Oxford, UK, pp. 55–74.

    Google Scholar 

  • Gupta M. N. 1991. Thermostabilization of proteins. Biotecimol. Appl. Biochem. 14: 1–11.

    Google Scholar 

  • Hayashi J. and Shimidzu Y. 1988. Patent IP 01249801 A2 891 005.

  • Hebeish A. and Waly A. 1978. Preparation of chemically modified cotton via introduction of aromatic amino-groups. J. Appl. Polym. Sci. 22: 2713–2716.

    Google Scholar 

  • Heinze Th., Rahn K., Jaspers M. and Berghmans H. 1996. p-Toluenesulfonyl esters in cellulose modifications: acylation of remaiiñng hydroxyl groups. Macromol. Chem. Phys. 197: 4207–4224.

    Google Scholar 

  • Hermanson G. T., Mallia A. K. and Smith P. K. 1992. Immobilized Affinity Ligand Tecimics. Academic Press, Inc., San Diego, California.

    Google Scholar 

  • Ikeda T., Katasho I., Kamei M. and Senda M. 1984. Electrocatalysis with a glucose-oxidase-immobilized graphite electrode. Agric. Biol. Chem. 48: 1969–1976.

    Google Scholar 

  • Ishii T. 1986. Facile preparation of deoxyiodocellulose and its conversion into 5, 6-cellulosene. Carbohydr. Res. 154: 63–70.

    Google Scholar 

  • Karube I. and Yokoyama K. 1993. Trends in biosensor research and development. Sensors Actuators B 13–14: 12–15.

    Google Scholar 

  • Karube I., Sode K. and Tamiya E. 1990. Microbiosensors for clin-ical analyses. In: Wise D. L. (ed), Bioinstrumentation-Research, Development and Applications. Butterworth, Inc., Boston, Massachusetts.

    Google Scholar 

  • Kierstan M. P. J. and Coughlan 1985. Immobilisation of cells and enzymes by gel entrapment. In: Woodward J. (ed), Immobilised Cells and Enzymes-A Practical Approach. IRL Press Ltd., Oxford, UK, pp. 39–48.

    Google Scholar 

  • Klavins M., Zicmanis A. and Prikulis A. 1984. Latv. PSR Zinat. Akad. Vestis Kim. Ser. 3: 336.

    Google Scholar 

  • Klei H. E., Sundstrom D. W. and Shim D. 1985. Immobilisation of enzymes by micro-encapsulation. In: Woodward J. (ed), Immobilised Cells and Enzymes-A Practical Approach. IRL Press Ltd., Oxford, UK, pp. 49–54.

    Google Scholar 

  • Li J.-ni, Du Y. ke, Boullanger P. and Jiang L. 1999. Thefolding and enzymatic activity of glucose oxidase in the glycolipid matrix of different charges. Thin Solid Films 352: 213–217.

    Google Scholar 

  • Malikkides C. O. and Weiland R. H. 1982. On the mechanism of immobilized glucose oxidase deactivation by hydrogen perox-ide. Biotechnol. Bioeng. 24: 2419–2439.

    Google Scholar 

  • Mannhalter Ch. 1993. Biocompatihility of artificial surfaces such as cellulose and related materials. Sensors Actuators B 11: 273–279.

    Google Scholar 

  • March W. F. 1990. Glucose biosensors. In: Wise D. L. (ed), Bioinstrnmentation-Research, Development and Applications. Butterworth, Inc., Boston, Massachusetts.

    Google Scholar 

  • McCormick C. L. and Callais P. A. 1987. Derivatization of cellulose in lithiumchloride and N, N-dimethylacetamide solutions. Polymer 28: 2317–2323.

    Google Scholar 

  • McCormick C. L., Dawsey T. R. and Newman J. K. 1990. Competitive formation of cellulose-p-toluenesulfonate and chlorodeoxycellulose during homogeneous reaction of p-toluene-sulfonyl chloride with cellulose in N, N-dimethylace-tamide-lithium chloride. Carbohydr. Res. 208: 183–190.

    Google Scholar 

  • Mikkelsen S. R. and Lennox R. B. 1991. Rotating disk electrode characterization of immobilized glucose oxidase. Anal. Biochem. 195: 358–363.

    PubMed  Google Scholar 

  • Mizutari F. and Asai M. 1990. Trends in enzyme sensors. In: Wise D. L. (ed), Bioinstrumentation-Research, Development and Applications. Butterworth, Inc., Boston, Massachusetts.

    Google Scholar 

  • Mosbach K. 1988. Immobilized enzymes and cells. In: Colowick S. P. and Kaplan N. O. (eds.), Methods in Enzymology, Vol. 137. Academic Press, Inc., San Diego, California.

    Google Scholar 

  • Nakamura S., Amano M., Saegusa Y. and Sato T. 1992. Preparation of aminoallcyl cellulose and their adsorption and resorption of heavy-metal ions. J. Appl. Polym. Sci. 45: 265–271.

    Google Scholar 

  • Ngo T. T., Ivy J. and Lenhoff H. M. 1980. Polyethylene beads as supports for enzyme immobilization. Biotechnol. Lett. 2: 429–434.

    Google Scholar 

  • Nilsson K. G. I. and Mandethus C. F. 1994. A carbohydrate bio-sensor surface for the detection of uropathogenic bacteria. BioTechnology 12: 1376–1378.

    PubMed  Google Scholar 

  • Ohba R., Shibata T. and Ueda 5. 1979. Preparation and properties of covalently immobilized beta-amylase on para aminobenzyl-cellulose. J. Ferment. Technol. 57: 146–150.

    Google Scholar 

  • Palmisano F., de Santis A., Tantfflo G., Voloicella T. and Zambonin P. G. 1997. Microbial detection by a glucose biosensor coupled to a microdialysis fibre. Analyst 122: 1125–1128.

    PubMed  Google Scholar 

  • Pazur J. H., Knull H. R. and Simpson L. 1970. Glycoenzymes: A note on the role for the carbohydrate moieties. Biochem. Biophys. Res. Commun. 40: 110–115.

    PubMed  Google Scholar 

  • Pyun J. C., Jang A. S. and Park J. S. 1996. Facile enzyme immobili-zation and assay techthque using polyethyleneimine-cellulose thin-layer chromatography as a solid support. Enzyme Microb. Technol. 18: 41–44.

    Google Scholar 

  • Racek J. 1991. A yeast biosensor for glucose determination. Appl. Microbiol. Biotechnol. 34: 473–477.

    PubMed  Google Scholar 

  • Rahn K., Diamantoglou M., Klemm D., Berghmans H. and Heinze Th. 1996. Homogeneous synthesis of cellulose-p-toluenesulfonates in N, N-dimethylacetamide/LiCI solvent system. Angew. Makromol. Chem. 238: 143–163.

    Google Scholar 

  • Rieseler R. 2001. Analyt-sensitive Nanostrnktur-Schichten fur die Biosensor-Entwicklung auf funktionalisierter Aminocellulosen-und SiOx-Polymerbasis. Dissertation Thesis, Forschungszentrnm Jiilich and RWTH Aachen, Germany.

    Google Scholar 

  • Sansubrino A. and Masciri M. 1994. Development of an optical fiber sensor for ammonia, urease and IgG. Biosens. Bioelectron. 9: 207–216.

    PubMed  Google Scholar 

  • Scouton W. H. 1987. A survey of enzyme coupling techniques. In: Mosbach K. V. (ed.), Methods in Enzymology, Vol. 135: Immobilized Enzymes and Cells Part B. Academic Press Inc., San Diego, California.

    Google Scholar 

  • Senda M. and Ikeda T. 1990. Biocatalyst electrodes and their capabilities for sensors and reactors. In: Wise D. L. (ed.), Bioinstrumentation-Research, Development and Applications. Butterworth, Inc., Boston, Massachusetts.

    Google Scholar 

  • Simionescu C. I., Dimitriu S., Popa M. I. and Denisova L. 1985. Antibiotics immobilized on polysaccharides. Makromol. Chem. Suppl. 9, 179–187.

    Google Scholar 

  • Steinberg R., Bindra D. S., Wilson G. S. and Thevenot D. R. 1988. Covalent enzyme coupling on cellulose acetate membranes for glucose sensor development. Anal. Chem. 60: 2781–2788.

    PubMed  Google Scholar 

  • Subramarian A., Kennel S. J., Oden P. 1., Jacobson K. B., Woodward J. and Doktycz M. J. 1999. Comparisonoftechthques for enzyme immobilization on silicon supports. Enzyme Microb. Technol. 24: 26–34.

    Google Scholar 

  • Tang L. X. and Vadgama P. M. 1990. Use of membrane techthque for optimization of enzyme electrodes. In: Wise D. L. (ed.), Bioinstrumentation-Research, Development and Applications. Butterworth, Inc., Boston, Massachusetts.

    Google Scholar 

  • Teshirogi T., Yamamoto H., Sakmoto M. and Tonami H. 1979. Sen-i Gakkaishi 35: T-525.

    Google Scholar 

  • Tifier J. 1999. Mai3geschneiderte Aminocellulosederivate zum Aufbau supramolekularer Cellulosearchitekturen mit Analyt-Erkennungsfunktion und optischer Signalgruppe. Dissertation Thesis, Forschungszentrnm Jiilich and Friedrich-Schiller-Universitat Jena, Germany.

    Google Scholar 

  • Tifier J., Berlin P. and Klemm D. 1999a. Soluble and film-forming cellulose derivates with redoxchromogethc and enzyme immo-bilizing 1, 4-phenylendiamine groups. Macromol. Chem. Phys. 200: 1–9.

    Google Scholar 

  • Tifier J., Berlin P. and Klemm D. 1999b. A novel efficient enzyme immobilization on NH2 polymers by means of L-ascorbic acid. Biotechnol. Appl. Biochem. 30: 155–162.

    PubMed  Google Scholar 

  • Tifier J., Berlin P. and Klemm D. 2000. Novel matrices for bio-sensor applications by strnctural design of redox-chromogenic aminocellulose esters. J. Appl. Polym. Sci. 75: 904–915.

    Google Scholar 

  • Tifier J., Klemm D. and Berlin P. 2001. Designed aliphatic amino-cellulose derivatives as transparent and functionalized coatings for enzyme immobilization. Design Monom. Polym. 4: 315–328.

    Google Scholar 

  • Tifier J., Rieseler R., Berlin P. and Klemm D. 2002. Stabilization of activity of oxido-reductases by their immobilization onto spe-cial functionalized glass and novel aminocellulose films using different coupling reagents. Biomacromolecules 3: 1021–1029.

    PubMed  Google Scholar 

  • Tokar O., Novak J. and Strakova V. 1981. Patent CS 223 256 B 86015. Chem. Abstr. 1986, 105, 81016w.

  • Towe P. C., Guilbeau E. J. and Coburn J. B. 1996. Invivo andinvitro deactivation rates of PTFE-coupled glucose oxidase. Biosens. Bioelectr. 11: 791–798.

    Google Scholar 

  • Tsuchida T. and Yoda K. 1983. Multi-enzyme membrane electrodes for determination of creatiiñne and creatine in scram. Chin. Chem. 29: 51–55.

    Google Scholar 

  • Tsuchida T. and Yoda K. 1981. Immobilization of D-glucose oxi-dase onto a hydrogen peroxide permselective membrane and application for an enzyme electrode. Enzyme Microb. Technol. 3: 326–330.

    Google Scholar 

  • Tsukamoto T., Nomura H., Morota S. and Okada 1. 1983. Kinetic studies on the oxidation of glucose by immobilized glucose oxidase. Chem. Phaim. Buli. 31: 3377–3384.

    Google Scholar 

  • Ulman A. 1991. An Introduction to Ultrathin Organic Films, LB Films in Sensors. Academic Press Inc., San Diego, California, p. 382.

    Google Scholar 

  • Ugarova N. N., Brovko Y. and Beiaieva Z Ed. 1983. Immobilization of luciferase from the firefly Luciola iningrelica: catalytic properties and thermostability of the enzyme immobilized on cellulose films. Enzyme Microb. Technol. 5: 60–65.

    Google Scholar 

  • Urban G. 1999. Microstnicturing of organic layers for microsys-tems. Sensors Actuators 74: 219–224.

    Google Scholar 

  • Valentova O., Marek M., Svec F., Stamberg J. and Vondrazka Z. 1981. Comparison of different methods of glucose-oxidase immobilization. Biotechnol. Bioeng. 23: 2093–2104.

    Google Scholar 

  • Vaima A. J. and Chavan V. B. 1994. Cellulosic diamines as reaction-incorporated fillers in epoxy composites. Cellulose 1: 215–219.

    Google Scholar 

  • Vegamd G. and Christensen T. B. 1975. Glycosylation of proteins-new method of enzyme stabilization. Biotechnol. Bioeng. 17: 1391–1397.

    PubMed  Google Scholar 

  • Vrbova E. and Marek M. 1990. Application of the Ugi reaction for the preparation of enzyme electrodes. Anal. Chim. Acta 239: 263–268.

    Google Scholar 

  • Weigl B. H., Holobar A., Rodriges N. Y. and Wolfbeis 0. 1993. Robust carbon dioxide optrode based on covalently immobilized pH indicator. SPIE 2068: 22ff.

    Google Scholar 

  • Wolfbeis O. S. 1991. Fiber Optic Chemical Sensors and Biosensors. Vol. 1 and 2, CRC Press, Inc., Boston, Massachusetts.

    Google Scholar 

  • Woodward J. 1985. Immobilised enzymes: adsorption and covalent coupling. In: Woodward J. (ed), Immobiised Cells and Enzymes-A Practical Approach. IRL Press Ltd., Oxford, UK, pp. 3–17.

    Google Scholar 

  • Wykes J. R., Dumñl P. and Lffly M. D. 1971. Immobiisation of alpha-amylase by attachment to soluble support materials. Biochim. Biophys. Acta 250: 522–529.

    PubMed  Google Scholar 

Download references

Author information

Author notes

  1. J. Tiller

    Present address: Freiburger Materialforschungszentrum, Albert-Ludwigs-Universität, Stefan-Meier-Str. 21, D-79104, Freiburg i. Br., Germany

Authors and Affiliations

  1. Forschungszentrum Jülich GmbH, ISG-2, D-52425, Jülich, Germany

    P. Berlin, A. Jung, R. Rieseler & J. Tiller

  2. Institut für Organische Chemie und Makromolekulare Chemie, Friedrich-Schiller-Universität, Lessingstraße 8, D-07743, Jena, Germany

    D. Klemm, H. Liebegott & J. Tiller

Authors
  1. P. Berlin
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. D. Klemm
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. A. Jung
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. H. Liebegott
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. R. Rieseler
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. J. Tiller
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to P. Berlin.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Berlin, P., Klemm, D., Jung, A. et al. Film-Forming Aminocellulose Derivatives as Enzyme-Compatible Support Matrices for Biosensor Developments. Cellulose 10, 343–367 (2003). https://doi.org/10.1023/A:1027342027945

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1023/A:1027342027945

Search

Navigation