caa a22 4500 467948887 CHVBK 20180405193740.0 cr unu---uuuuu 170328e20050201xx s 000 0 eng 10.1023/B:CELL.0000049351.44348.30 doi (NATIONALLICENCE)springer-10.1023/B:CELL.0000049351.44348.30 (NATIONALLICENCE)springer-10.1007/s10570-004-4356-9 New water-soluble and film-forming aminocellulose tosylates as enzyme support matrices with Cu2+-chelating properties [Elektronische Daten] [A. Jung, P. Berlin] 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 (<1nm), 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 K M value, can be changed by the interplay of aminocellulose film, coupling structure and enzyme protein in the sense of an application-relevant optimization. Kluwer Academic Publishers, 2005 Aminocellulose derivatives nationallicence Atomic force microscopy nationallicence Enzyme coupling nationallicence Thin films nationallicence ABTS : 2,2′-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) nationallicence AFM : atomic force microscopy nationallicence AGU : anhydroglucose unit nationallicence APTMS : 3-aminopropyltrimethoxysilane nationallicence DETA : diethylenetriamine nationallicence DMA : N,N-dimethylacetamide nationallicence DMSO : dimethylsulfoxide nationallicence DPTA : dipropylenetriamine nationallicence DS : degree of substitution nationallicence EDA : ethylenediamine nationallicence GOD : glucose oxidase nationallicence HDA : hexylenediamine nationallicence HRP : horseradish peroxidase nationallicence MPTEOS : methacrylpropyltriethoxysilane nationallicence SPR : surface plasmon resonance nationallicence TETA : tetraethylene tetramine nationallicence THF : tetrahydrofuran nationallicence Jung A. ISG-2, Forschungszentrum Juelich GmbH, D-52425, Juelich, Germany aut Berlin P. ISG-2, Forschungszentrum Juelich GmbH, D-52425, Juelich, Germany aut Cellulose Kluwer Academic Publishers 12/1(2005-02-01), 67-84 0969-0239 12:1<67 2005 12 10570 https://doi.org/10.1023/B:CELL.0000049351.44348.30 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1023/B:CELL.0000049351.44348.30 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Jung A. ISG-2, Forschungszentrum Juelich GmbH, D-52425, Juelich, Germany aut NATIONALLICENCE 700 1- Berlin P. ISG-2, Forschungszentrum Juelich GmbH, D-52425, Juelich, Germany aut NATIONALLICENCE 773 0- Cellulose Kluwer Academic Publishers 12/1(2005-02-01), 67-84 0969-0239 12:1<67 2005 12 10570 NATIONALLICENCE 700 1- Jung A. Forschungszentrum Juelich GmbH ISG-2, D-52425, Juelich, Germany aut NATIONALLICENCE 700 1- Berlin P. Forschungszentrum Juelich GmbH ISG-2, D-52425, Juelich, Germany aut NATIONALLICENCE 856 40 https://doi.org/10.1007/s10570-004-4356-9 text/html Onlinezugriff via DOI Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE NATIONALLICENCE NL-springer