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  • 1
    Electronic Resource
    Electronic Resource
    The photochemically-induced grafting of styrene onto cellulose in the homogeneous styrene/cellulose/ D.M.S.O./HCHO system (1979)
    Springer
    Polymer bulletin 1 (1979), S. 501-508 
    Details
    ISSN: 1436-2449
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Synopsis Styrene has been successfully grafted onto cotton cellulose under ‘homogeneous’ conditions provided by initial methylolation using the cellulose/DMSO/HCHO system. The attendant homopolymerization reaction has also been examined. Both grafting and homopolymerization show a rapid initial rate which appears to level off. The homopolymerization reaction increases with increasing concentration of styrene in the medium. Grafting is seen to maximize with increasing bulk monomer concentration, the position of the maximum showing some dependence on the exposure time, under otherwise standard conditions. These observations are interpreted in terms of increasingly restricted access of the monomer into the substrate, arising from the grafting process, which reduces the level of solubility of the methylol cellulose-polystyrene graft copolymer entity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00255715
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  • 2
    Electronic Resource
    Electronic Resource
    Investigation of the immobilisation of bovine serum albumin, trypsin, acid phosphatase and alkaline phosphatase to poly(hydroxyethyl acrylate)-co-cellulose and poly(hydroxyethyl acrylate)-co-pectin (1984)
    Springer
    Polymer bulletin 11 (1984), S. 1-6 
    Details
    ISSN: 1436-2449
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Summary Poly(hydroxyethyl methacrylate)-co-pectins (107% graft), activated with p-benzoquinone, immobilised 122 mg of bovine serum albumin (BSA) per g of copolymer and 22.4 mg of trypsin per g of copolymer. This latter figure was replicated when p-toluene sulphonyl chloride was used for activating the copolymer. In a separate exercise p-benzoquinone was used to couple diaminohexane to the copolymer. This modified product immobilsed 396 mg of trypsin/g when glutaraldehyde was used in coupling. A 25% grafted, poly(hydroxyethyl methacrylate)-co-cellulose immobilised 39.5 mg of BSA per g of copolymer.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00401706
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  • 3
    Electronic Resource
    Electronic Resource
    The use of graft copolymers as enzyme supports (1980)
    Springer
    Polymer bulletin 3 (1980), S. 645-653 
    Details
    ISSN: 1436-2449
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Summary A study has been made of the radiation-induced grafting of acrylic acid onto polyethylene. Grafting was found to be steady state in character in the early stages, when carried out in a suitable medium. Evidence is presented showing that, in the later stages, autoacceleration becomes a feature of the grafting process. Thermal analysisprocedures were used in an attempt to show the occurrence of grafting. Immobilization using N-ethoxycarbonyl-2-ethoxy,-1,2-dihydroquinoline (EEDQ) as the coupling agent was attempted. This met with various levels of success. The copolymer-EEDQ-enzyme system was used to couple bovine serum albumin (65 mg protein/g of substrate) and phenyl propylamine (95 mg phenylpropylamine/g of substrate).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00285301
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  • 4
    Electronic Resource
    Electronic Resource
    The use of graft copolymers as enzyme supports (1980)
    Springer
    Polymer bulletin 2 (1980), S. 607-612 
    Details
    ISSN: 1436-2449
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Summary The grafting of acrylonitrile on to nylon powder was carried out in DMF solution after vacuum impregnation. Initiation was radiation induced. A sample of graft copolymer was reduced and coupled to enzyme using a water soluble carbodi-imide, or using glutaraldehyde. Some samples of the graft copolymer were selectively hydrolysed to the corresponding acrylic acid form and used for coupling to bovine serum albumin, invertase, pepsin, acid and alkaline phosphate, using water soluble carbodi-imides.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00263031
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  • 5
    Electronic Resource
    Electronic Resource
    The use of graft copolymers as enzyme supports (1979)
    Springer
    Polymer bulletin 1 (1979), S. 749-753 
    Details
    ISSN: 1436-2449
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Summary A new type of polymer support for immobilizing enzymes, a copolymer grafted onto nylon was investigated. Polyacrylamide was used and successfully coupled to β-galactosidase (from yeast and bacteria) using two different methods to give activities of the order of 5 units/g of polymer for the yeast enzyme, and 156 units/g for the E.coli enzyme. Lactose did not affect the yield. The azide method gave better results than the glutaraldehyde method. β-galactosidase coupled enzyme was fairly stable but not as good as the free enzyme. Papain was also coupled to the polyacrylamide grafted nylon using both methods; the glutaraldehyde gave better results with 1.5mg of enzyme being coupled for each gram of polymer.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00256275
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  • 6
    Electronic Resource
    Electronic Resource
    The use of graft copolymers as enzyme supports (1979)
    Springer
    Polymer bulletin 1 (1979), S. 755-761 
    Details
    ISSN: 1436-2449
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Summary β-Galactosidase and glucose oxidase have been immobilized on cellulose-polyacrylamide (C-PAM) graft copolymers, using the azide method or through glutaraldehyde. The original (C-PAM) copolymers were prepared via radiation-induced grafting under controlled conditions by both post-irradiation and simultaneous procedures. The optimum conditions for coupling of the copolymers to the enzymes were established as were the levels of activity of the immobilized enzymes. Grafting by the simultaneous route was seen to be more efficient than postirradiation grafting. Indirect evidence of grafting was found from elemental and thermal analysis. Binding of β-galactoside was found to be more successful than that of glucose oxidase. A relationship between the level of immobilized enzyme activity and the extent of grafting in the copolymer was established for the β-galactosidase system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00256276
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  • 7
    Electronic Resource
    Electronic Resource
    The immobilisation of bovine serum albumin, acid phosphatase, glucose oxidase and phenyl propylamine to maleic anhydride block copolymers (1985)
    Springer
    Polymer bulletin 14 (1985), S. 199-206 
    Details
    ISSN: 1436-2449
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Summary Maleic anhydride-based block copolymers have been prepared by various routes. These copolymers provide the basis for enzyme immobilisation without the need for secondary coupling agents. It is felt that problems arising from enzyme-support interactions are much reduced relative to systems using poly(acrylic acid)-branch supports. There are problems in stability in that these supports cannot be used above a pH of 7.4. At low pH values, gel formation arises. Such gel formation enhances the immobilisation efficiency considerably but generates media which are difficult to process. Ease of coupling was a feature of non-aqueous systems, suggesting that products obtained in this way should be of use in affinity separations.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00254938
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  • 8
    Electronic Resource
    Electronic Resource
    Investigation of the coupling of water soluble poly(acrylic acid) and poly(methacrylic acid) to amines and to β-galactosidase (1981)
    Springer
    Polymer bulletin 4 (1981), S. 149-156 
    Details
    ISSN: 1436-2449
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Summary Acrylic acid and methacrylic acid were polymerized by γ — irradiation to give homogeneous solution of homopolymer. Neither homopolymeric species coupled to benzylamine or phenylpropylamine with water soluble carbodi-imides or Woodward's K Reagent but both homopolymers coupled to β — galactosidase using a water soluble carbodi-imide. In each instance, the activity of the enzyme was unaffected. Evidence for the formation of covalent links between the enzyme and the copolymer was obtained from electrophoresis and by analyzing the products obtained by precipitation of the enzyme-copolymer complexes. Both homopolymer species markedly effected the activity of acid phosphatase without the condensing agent being present.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00263055
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  • 9
    Electronic Resource
    Electronic Resource
    Characterization of cellulose derivatives — Relevance to sensor development (1995)
    Springer
    Cellulose 2 (1995), S. 243-263 
    Details
    ISSN: 1572-882X
    Keywords: cellulose acetate ; cellulose acetate butyrate ; ethyl cellulose ; characterization ; biosensor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract With the aim of developing a urea biosensor, several cellulose derivatives were used to coat an all-solid-state potentiometric electrode for ammonium ion determination. In this work the physical and chemical characterization of the cellulose derivatives, as well as the changes that the activation and immobilization procedures induced in the polymers, were studied.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00811816
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  • 10
    Electronic Resource
    Electronic Resource
    Immobilization of β-galactosidase and other enzymes onto p-amino-carbanilated cellulose derivatives (1980)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 22 (1980), S. 311-321 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: β-Galactosidase and other enzymes were immobilized on p-amino-carbanilated derivatives of cellulose and methylol cellulose using the diazo method and through glutaraldehyde. The optimum conditions for coupling cellulose tri-(p-amino-carbanilate) (CTAC) to β-galactosidase were established. The diazo coupling method with CTAC gave greater activity than with glutaraldehyde when coupled to β-galactosidase (Escherichia coli). The stability of the CTAC-β-galactosidase system was examined. The disubstituted p-amino-carbanilate derivative (CDAC) gave a lower activity, whereas the methylol analog (MCTAC) gave slightly greater activity. The CTAC was also used to immobilize glucose oxidase, trypsin, pepsin, and papain.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260220206
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