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  • Wiley-Blackwell  (11)
  • 1980-1984  (11)
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Publisher
Years
Year
  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Applied Polymer Science 28 (1983), S. 2167-2175 
    ISSN: 0021-8995
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: The influence of the hydrratin ability of monomer on the immobilization of microbial cells by radiation polymerization was studied using various acrylate and diacrylate monomers. The heats of mixing of the monomers in water were determined, and the hydratin abilities of monomer and polymer were evaluated by heat of mising and water content. The shape of the immobilized cell composites varied with the hydratin ability of monomer. The enzymatic activity of the immobilized cell composites varied with the number of ethyleneglycol or methylene units in the monomers. In the immobilization using acrylate monomers, the increase of the hydration ability of the monomer introduced a spongelike composite to the formation of the immobilized cells, and, in diacrylate monomers, the increase of the hydration ability of the monomer introduced a flakelike composite to the formation of the immobilized cells, by which enzymatic activity increased.
    Additional Material: 8 Ill.
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Applied Polymer Science 29 (1984), S. 2713-2718 
    ISSN: 0021-8995
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: A new method is discussed for the immobilization of cellulase using porous polymer matrices, which were obtained by radiation polymerization of hydrophilic monomers. In this method, the immobilized enzyme matrix was prepared by enzyme absorbtion in the porous polymer matrix and drying treatment. The enzyme activity of the immobilized enzyme matrix varied with monomer concentration, cooling rate of the monomer solution, and hydrophilicity of the polymer matrix, taking the change of the nature of the porous structure in the polymer matrix. The leakage of the enzymes from the polymer matrix was not observed in the repeated batch enzyme reactions.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 26 (1984), S. 17-21 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The cellulase production from immobilized Trichoderma reesei composites prepared by radiation polymerization at low temperature was studied. The production of cellulase from the cells irradiated by radiation was slightly retarded at the initial stage of the culture, but was immediately recovered. The production of cellulase resulting from the growth of the immobilized cells proceeds efficiently in the composite having a porous polymer matrix, in which the productivity of cellulase varied with the hydrophilicity, the shape of the composite, monomer, and cell concentration. It was found that cellulase produced by immobilized growing cell composites effectively hydrolyzed cellulosic wastes such as newspaper and chaff which are pretreated by irradiation and crushing.
    Additional Material: 7 Ill.
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Applied Polymer Science 28 (1983), S. 295-301 
    ISSN: 0021-8995
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Immobilization of Mortierella vinacea cells, which contain active α-galactosidase, by radiation polymerization at low temperatures was studied. The durability of the enzymatic activity of the immobilized cells was examined by repeating the batch enzyme reaction. The enzymatic activities of the immobilized cells obtained with hydrophilic monomers was affected by the concentrations of the cells and monomer in which optimum conditions were observed. The enzymatic activity of the immobilized cells obtained with hydrophilic monomer was compared to that of hydrophobic monomers. Michaelis constants of the immobilized cells varied with monomer concentration. The effect of addition of porous solid substances on the immobilization of the cells was studied.
    Additional Material: 8 Ill.
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Applied Polymer Science 28 (1983), S. 3759-3765 
    ISSN: 0021-8995
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Streptomyces phaeochromogenes cells were immobilized on cellulose-polymer surfaces by radiation polymerization using hydrophilic monomers and paper. The enzyme activity of immobilized cell sheets was higher than that of immobilized cell composites obtained by the usual radiation polymerization technique. The enzyme activity of the sheets was affected by monomer concentration, the thickness of paper, and the degree of polymerization of paper. The copolymerization of hydroxyethyl methacrylate and methoxytetraethyleneglycol methacrylate in the sheets led to a further increase of the enzyme activity due to the increase of the hydrophilicity of the polymer matrix. The Michaelis constant of the sheets from low monomer concentration was close to that of intact cells.
    Additional Material: 6 Ill.
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  • 6
    Electronic Resource
    Electronic Resource
    Hoboken, NJ : Wiley-Blackwell
    Journal of Biomedical Materials Research 14 (1980), S. 199-210 
    ISSN: 0021-9304
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine , Technology
    Notes: The immobilization of some medically useful enzymes were studied by means of radiation-induced polymerization at -78°C. Glucose oxidase and glucose peroxidase were immobilized in the form of thin membranes inside polyvinyl chloride tubes and on polyethylene films; these membranes showed considerable activity yield, as well as good activity retention. Two effective methods were adopted to improve the surface properties of the base materials and to facilitate firm immobilization by coating: that is, an undercoating method followed by radiation curing of the undercoating and an irradiation grafting method with a monomer. Both were tested with good results. An immobilization of urokinase was also carried out successfully by similar methods. The thrombogenicity of the immobilized urokinase showed a remarkable effect on thrombus formation.
    Additional Material: 8 Ill.
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  • 7
    ISSN: 0025-116X
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: Cellulase was immobilized on a porous polymer matrix which was formed by radiation polymerization of bifunctional monomers such as poly(ethylene glycol) diacrylates (1), and the nature of the porous polymer matrix and its effect on the enzymatic activity was studied. The porous structure of the polymer matrix was found to change markedly with the monomer concentration and irradiation temperature. The formation of the porous structure shows a discontinuous change in the temperature region of -10 to -40°C, due to the change in polymerization phase and mechanism. The enzymatic activity is strongly related to the pore size, the degree of hydration of the polymer matrix, and the particle size of the composite. The degree of hydration of the polymer matrix varies with the number of oxyethylene units in the monomers 1.
    Additional Material: 6 Ill.
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  • 8
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Angewandte Makromolekulare Chemie 115 (1983), S. 75-86 
    ISSN: 0003-3146
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Description / Table of Contents: Es wird über ein Verfahren zur Immobilisierung von Zellen mittels Strahlungs-Guß-Polymerisation berichtet. Die Immobilisierungsparameter, die die Enzymaktivität der immobilisierten Zellmembranen beeinflussen, wurden in absatzweisen Enzymreaktionen untersucht. Es handelte sich dabei um folgende Parameter: Monomerkonzentration, Membrandicke und Konzentration von Zusätzen. Die Michaelis-Konstante von immobilisierten Zellmembranen hängt von der Membrandicke und der Konzentration der Zusatzstoffe ab. Die Wärme- und pH-Stabilität der immobilisierten Zellmembaranen wurde untersucht.
    Notes: A method of cell immobilization by radiation-induced cast-polymerization is reported. Immobilization parameters which influence the enzymatic activity of immobilized cell membranes have been studied in batch enzyme reactions. These parameters are monomer concentration, membrane thickness and additive concentration. The Michaelis constant of immobilized cell membranes depends on the membrane thickness and additive concentration. The heat and pH stability of immobilized cell membranes was studied.
    Additional Material: 11 Ill.
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  • 9
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Helvetica Chimica Acta 66 (1983), S. 2044-2048 
    ISSN: 0018-019X
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Thermolysin was immobilized by radiation polymerization of hydroxyalkyl acrylate and tetradecaethylene glycol dimethacrylate monomers at low temperatures in the presence of the enzyme, and the degree of interaction of the enzyme with the polymer matrix was studied by measuring the thermal stability of the immobilized enzyme. The thermal stability was affected by the molecular structure of the monomer; the thermal stability of the immobilized enzyme from hydrophilic monofunctional monomers in the wet state was higher than that from hydrophobic bifunctional monomers. The thermal stability in polymers formed from hydroxy-alkyl acrylates decreased with an increase in the number of methylene units in the monomer, owing to a change of the state of the enzyme trapped in the porous polymer matrix. The enzyme molecule trapped in a hydrophilic porous polymer matrix appeared to be stabilized by interaction with the polymer chains.
    Additional Material: 3 Ill.
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  • 10
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Helvetica Chimica Acta 66 (1983), S. 2778-2784 
    ISSN: 0018-019X
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The immobilization of enzymes such as cellulase by radiation polymerization of dispersed polyurethane prepolymer was studied using tolylene-2,4-diisocyanate and 2-hydroxyethyl methacrylate. The polyurethane particles were obtained by the dispersion of polyurethane prepolymer followed by radiation polymerization, in which the enzyme was immobilized on its surface by convalent bonding. The particle diameter of immobilized enzyme particles varied with monomer concentration and composition. The enzymatic activity of immobilized enzyme particles varied with the temperature of dispersion and irradiation, and decreased with increasing particle diameter.
    Additional Material: 6 Ill.
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