Abstract
Within the framework of our studies on enzyme-compatible support matrix structures, we succeeded in making further derivatives of the new aminocellulose type ‘P–CH2–NH–(X)–NH2’ (P = cellulose); (X) = –(CH2)2– (EDA), –(CH2)2–NH–(CH2)2– (DETA), –(CH2)3–NH–(CH2)3– (DPTA), –(CH2)2–NH–(CH2)2–NH–(CH2)2– (TETA) accessible by nucleophilic substitution reaction with ethylenediamine (EDA) and selected oligoamines starting from 6(2)-O-tosylcellulose tosylate (DStosylate = 0.8). The 13C-NMR data show that the EDA and oligoamine residues are at C6 of the anhydroglucose unit (AGU) and that OH and tosylate are also (partially) present at C6. OH and partially tosylate are at C2/C3. All the synthesized aminocellulose tosylates were soluble in water and formed transparent films from their solutions. The aminocellulose tosylate solutions and the films prepared from them formed blue-coloured chelate complexes with Cu2+ ions, whose absorption maxima at wavelengths in the VIS region were located similarly to those of the Cu2+ chelate complexes with EDA and with the oligoamines. AFM investigations have shown that the aminocellulose films, depending on structural and environment-induced factors influencing e.g. SiO2 polymer films, exhibit ‘flat’ topographies (<1 nm), and on protonated NH2 polymer films, such as aminopropyl-functionalized polysiloxane films, ‘nanostructured’ topographies of derivative-dependent shape and nanostructure size as film supports in the form of ‘nanotubes’. The aminocellulose films could be covalently coupled with glucose oxidase enzyme by various known and novel bifunctional reactions via NH2-reactive compounds. In this connection, it was confirmed again that the immobilized enzyme parameters, such as enzyme activity/area and KM value, can be changed by the interplay of aminocellulose film, coupling structure and enzyme protein in the sense of an application-relevant optimization.
Similar content being viewed by others
Abbreviations
- ABTS:
-
2,2′-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid)
- AFM:
-
atomic force microscopy
- AGU:
-
anhydroglucose unit
- APTMS:
-
3-aminopropyltrimethoxysilane
- DETA:
-
diethylenetriamine
- DMA:
-
N,N-dimethylacetamide
- DMSO:
-
dimethylsulfoxide
- DPTA:
-
dipropylenetriamine
- DS:
-
degree of substitution
- EDA:
-
ethylenediamine
- GOD:
-
glucose oxidase
- HDA:
-
hexylenediamine
- HRP:
-
horseradish peroxidase
- MPTEOS:
-
methacrylpropyltriethoxysilane
- SPR:
-
surface plasmon resonance
- TETA:
-
tetraethylene tetramine
- THF:
-
tetrahydrofuran
References
M. Alvarez-Icaza H.M. Kalisz H.J. Hecht K.-D. Aumann D. Schomburg R.D. Schmid (1995) ArticleTitleThe design of enzyme sensors based on the enzyme structure Biosens. Bioelectron. 10 735–742
A.V. Barmin A.V. Eremenko A.A. Sokolovskij S.F. Chernov I.N. Kurochkin (1993) ArticleTitleNew catalytic properties of glucose oxidase in monomolecular films Biotechnol. Appl. Biochem. 18 369–376
P. Berlin J. Tiller R. Rieseler D. Klemm (1998) ArticleTitleSupramolekulare Erkennungsstrukturen auf Cellulosebasis Das Papier 52 737–742
P. Berlin D. Klemm J. Tiller R. Rieseler (2000) ArticleTitleFeature – a novel soluble aminocellulose derivate type: its transparent film-forming properties and its efficient coupling with enzyme proteins for biosensors Macromol. Chem. Phys. 201 2070–2082
P. Berlin D. Klemm A. Jung H. Liebegott R. Rieseler J. Tiller (2003) ArticleTitleReview – Film-forming aminocellulose derivatives as enzyme-compatible support matrices for biosensor developments Cellulose 10 343–367
J. Chibatu (1978) Preparation of Immobilized Enzymes and Microbial Cells. Main entry under title: Immobilized Enzymes, Research and Development Kodanska Scientific Books TokyoJapan and Halsted Press, New York
A.R. Comfort E. Albert R. Langer (1989) ArticleTitleImmobilized enzyme cellulose hollow fibers: immobilization of heparinase Biotechnol. Bioeng. 34 1366–1374
J.V. Daele J.-F. Revol F. Gaill G. Coffinet (1992) ArticleTitleCharacterization of supramolecular architecture of the cellulose-protein in the tunic sea peach J. Biol. Cell 76 87–96
H. Gallati (1979) ArticleTitleHorseradish-peroxidase – study of the kinetics and the determination of optimal reaction conditions, using hydrogen-peroxide and 2,2-azino-bis-3-ethylbenzthiazoline-6-sulfonic acid (ABTS) as substrates J. Clin. Chem. Clin. Biochem. 17 1–7
L. Goldstein (1976) Kinetic behavior of immobilized enzyme systems K. Mosbach (Eds) Immobilized Enzymes. Methods in Enzymology Academic Press New York 397–443
A.P.A. Goncalves M.B.F. Martins M.E.M. Cruz (1991) ArticleTitleAnalytical use of immobilized glucose oxidase – kinetic and operational studies Appl. Biochem. Biotechnol. 27 139–143
W. Göpel (1994) ArticleTitleNew materials and transducers for chemical sensors Sensors Actuators B18–19 1–21
B.A. Gregg A.J. Heller (1991) ArticleTitleRedox-polymer films containing enzymes. 2. Glucoseoxidase containing enzyme electrodes J. Phys. Chem. 95 5976–5980
A. Jung P. Berlin B. Wolters (2004) ArticleTitleBiomolecule-compatible support structures for biomolecule coupling to physical measuring principle surfaces IEE Proc. Nanobiotechnol. 151 87–94
H.E. Klei D.W. Sundstrom D. Shim (1985) Immobilisation of enzymes by micro-encapsulation J. Woodward (Eds) Immobilised Cells and Enzymes – A Practical Approach IRL Press Ltd OxfordUK 49–54
J.-ru Li Y.-ke Diu P. Boullanger L. Giang (1999) ArticleTitleThe folding and enzymatic activity of glucose oxidase in the glycolipid matrix of different charges Thin Solid Films 352 213–217
Ch. Mannhalter (1993) ArticleTitleBiocompatibility of artificial surfaces such as cellulose and related materials Sensors Actuators B11 273–279
K. Mosbach (1988) Immobilized Enzymes and Cells. Methods in Enzymology Academic Press San DiegoCA
J.H. Parzur H.R. Knull L. Simpson (1970) ArticleTitleGlycoenzymes: a note on the role for the carbohydrate moieties Biochem. Biophys. Res. Commun. 40 110–115
R. Rieseler 2001 Analyt-sensitive Nanostrukturschichten für die Biosensor-Entwicklung auf funktionalisierter Aminocellulosen und SiOx Polymerbasis. Dissertation Thesis Forschungszentrum Juelich GmbH and RWTH Aachen. Germany
A. Sansubrino M. Mascini (1994) ArticleTitleDevelopment of an optical fiber sensor for ammoniaurease and IgG Biosens. Bioelectron. 9 207–216
D.S. Sternberg Bindra G.S. Wilson D.R. Thevenot (1988) ArticleTitleCovalent enzyme coupling on cellulose acetate membranes for glucose sensor development Anal. Chem. 60 2781–2788
Tiller J. 1999. Maßgeschneiderte Aminocellulosederivate zum Aufbau supramolekularer Cellulose-Architekturen mit Analyt-Erkennungsfunktion und optischer Signalgruppe. Dissertation Thesis, Friedrich-Schiller-Universität Jena/Forschungszentrum JülichGermany.
J. Tiller P. Berlin D. Klemm (1999a) ArticleTitleSoluble and film-forming cellulose derivates with redoxchromogenic and enzyme immobilizing 1,4-phenylendiamine groups Macromol. Chem. Phys. 200 1–9
J. Tiller P. Berlin D. Klemm (1999b) ArticleTitleNovel efficient enzyme immobilization on NH2 polymers by means of l-ascorbic acid Biotechnol. Appl. Biochem. 30 IssueID2 155–162
J. Tiller P. Berlin D. Klemm (2000) ArticleTitleNovel matrices for biosensor applications by structural design of redox-chromogenic aminocellulose esters J. Appl. Polymer Sci. 75 904–915
J. Tiller D. Klemm P. Berlin (2001) ArticleTitleDesigned aliphatic aminocellulose derivatives as transparent and functionalized coatings for enzyme immobilization Des. Monomers Polym. 4 315–328
J. Tiller R. Rieseler P. Berlin D. Klemm (2002) ArticleTitleStabilization of activity of oxidoreductases by their immobilization onto special functionalized glass and novel aminocellulose film using different coupling reagents Biomacromolecules 3 1021–1029
G. Vegarnd T.B. Christensen (1975) ArticleTitleGlycosylation of proteins – new method of enzyme stabilization Biotechnol. Bioeng. 17 1391–1397
B.H. Weigl A. Holobar N.V. Rodriges O. Wolfbeis (1993) ArticleTitleRobust carbon dioxide optrode based on covalently immobilized pH indicator Proc. SPIE 2068 22ff
J. Woodward (1985) Immobilised enzymes: adsorption and covalent coupling J. Woodward (Eds) Immobilised Cells and Enzymes – A Practical Approach IRL Press Ltd OxfordUK 3–17
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Jung, A., Berlin, P. New water-soluble and film-forming aminocellulose tosylates as enzyme support matrices with Cu2+-chelating properties. Cellulose 12, 67–84 (2005). https://doi.org/10.1007/s10570-004-4356-9
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/s10570-004-4356-9