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  • Chemistry  (24)
  • 2015-2019
  • 1975-1979  (22)
  • 1950-1954  (2)
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  • 1
    Electronic Resource
    Electronic Resource
    The synthesis of monomers that expand on polymerization. Synthesis and polymerization of 8,10,19,20-tetraoxatrispiro[5.2.2.5.2.2]heneicosane (1976)
    New York : Wiley-Blackwell
    Die Makromolekulare Chemie 177 (1976), S. 3231-3235 
    Details
    ISSN: 0025-116X
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Description / Table of Contents: Das Spiroorthocarbonat, 8,10,19,20-Tetraoxatrispiro[5.2.2.5.2.2]heneicosan (1), welches zwei Cyclohexylgruppen enthält, wurde dargestellt. Das Monomere wurde mittels eines kationischen Katalysators wie Bortrifluoridätherat oder Zinn(IV)-chlorid polymerisiert. Die Struktur des Polymeren wurde mit Hilfe der IR und NMR Spektren bestimmt; es sind Copolymere mit alternierenden Äther- und Carbonatverknüpfungen. Das Monomere 1 expandiert bei der Polymerisation.
    Notes: A spiro orthocarbonate containing two cyclohexyl groups, 8,10,19,20-tetraoxatrispiro[5.2.2.5.2.2]heneicosane (1), was prepared. The monomer was polymerized with Lewis acids such as boron trifluoride etherate or stannic chloride as catalysts. The IR and NMR spectra indicated that the polymer was an alternating copolymer with ether and carbonate linkages. This monomer underwent expansion on polymerization.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/macp.1976.021771111
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  • 2
    Electronic Resource
    Electronic Resource
    Synthesis of monomers expanding on polymerization. Synthesis and polymerization of 3-methylene-1,5,7,11-tetraoxaspiro[5.5]undecane (1975)
    New York : Wiley-Blackwell
    Die Makromolekulare Chemie 176 (1975), S. 2897-2903 
    Details
    ISSN: 0025-116X
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Description / Table of Contents: Ein Spiro-orthocarbonat, das eine Doppelbindung enthält [3-Methylen-1,5,7,11-tetraoxaspiro[5.5]undecan (2)], wurde aus 2-Methylen-1,3-propandiol dargestellt. Die Struktur von 2 wurde elementaranalytisch sowie IR und NMR-spektroskopisch bestätigt. Das Monomer 2 wurde mittels eines kationischen Katalysators, Bortrifluoridätherat oder Zinntetrachlorid, polymerisiert. Aus den IR und NMR Spektren des Polymers geht hervor, daß es sich um ein alternierendes Copolymer mit Äther- und Carbonat-Bindungen handelt, das außerdem eine doppelt gebundene Seitengruppe enthält (Struktur 8). Das Monomer 2 erfährt eine Ausdehnung während der Polymerisation.
    Notes: A spiro ortho carbonate containing a double bond, 3-methylene-1,5,7,11-tetraoxaspiro-[5.5]undecane (2) was prepared from 2-methylene-1,3-propanediol. The structure of the monomer was confirmed by its elemental analysis, IR and NMR spectra. The monomer was polymerized with Lewis acids such as boron trifluoride etherate and stannic chloride (tin tetrachloride) as catalysts. The IR and NMR spectra indicated that the polymer has the structure of an alternating copolymer containing ether and carbonate linkages with a pendant double bond (structure 8).Monomer 2 underwent expansion on polymerization.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/macp.1975.021761011
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  • 3
    Electronic Resource
    Electronic Resource
    Immobilization of enzymes on activated carbon: Selection and preparation of the carbon support (1979)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 21 (1979), S. 461-476 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Based upon its superior catalytic activity for H2O2 decomposition, a bituminous coal-based activated carbon was selected for investigations of pretreatment and enzyme immobilization methods. Pretreatments considered include acid washing, exposure to strong oxidizing agents, contact with concentrated peroxide solutions, nitration and amination, isothiocyanate derivatization, silanization, and stearic acid coating. Effects of these pretreatments on morphology and trace-metal content of the carbon pellets have been studied using scanning electron microscopy and dispersive analysis of x rays. Immobilization of glucoamylase by adsorption, glutaraldehyde crosslinking, and covalent attachment to carbon activated by water-soluble diimide or diazotization have been examined. These different enzyme-carbon catalysts have been characterized by their enzyme loading, enzyme activity, catalytic activity for H2O2 decomposition, or combinations of these measures of performance.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260210308
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  • 4
    Electronic Resource
    Electronic Resource
    Enzyme immobilization on activated carbon: Alleviation of enzyme deactivation by hydrogen peroxide (1977)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 19 (1977), S. 769-775 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260190514
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  • 5
    Electronic Resource
    Electronic Resource
    Applications of purification reactions for minimizing reaction-generated enzyme poisoniong (1978)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 20 (1978), S. 1249-1265 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A mathematical model has been employed to examine the interplay of reaction and mass transfer in immobilized enzyme systems involving reaction-generated enzyme poisons. Deactivation rates can be significantly reduced in some cases by catalyzing a purification reaction in which the poison is transformed into an innocuous substance. This conclusion is illustrated experimentally for reaction-generated H2O2 in a continuous-flow stirred slurry reactor containing glucose oxidase immobilized on activated carbon.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260200810
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  • 6
    Electronic Resource
    Electronic Resource
    Diffusional influences on the parametric sensitivity of immobilized enzyme catalystsNCL Communication No. 2141. (1978)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 20 (1978), S. 1817-1831 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Immobilization of an enzyme within an insoluble material permeable to substrate can change the apparent behavior of the enzyme. In particular, external mass transfer and intraparticle diffusion effects can significantly influence the dependence of observed reaction rate on operating parameters such as temperature and pH. This analysis shows that, under very general conditions, the influence of diffusion alone is to diminish the sensitivity of the observed rate to any parameter that is uniform throughout the catalyst particle. However, the optimal value of the parameter is not changed because of intrapellet diffusional effects.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260201110
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  • 7
    Electronic Resource
    Electronic Resource
    The influence of peroxide-stabilizing agents on enzyme deactivation by H2O2 (1977)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 19 (1977), S. 157-158 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 1 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260190113
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  • 8
    Electronic Resource
    Electronic Resource
    Immobilization of enzymes on activated carbon: Properties of immobilized glucoamylase, glucose oxidase, and gluconolactonase (1978)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 20 (1978), S. 1651-1665 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Apparent kinetics and pH-activity relationships have been determined for glucoamylase and glucose oxidase immobilized on activated carbon using a diimide method. Reaction rate expressions of Michaelis-Menten form adequately approximate the observed kinetics for both enzyme preparations over the ranges of substrate concentrations considered. Influences of external mass transfer as well as substrate and product adsorption on interpretation of the experimental data have been examined. Immobilization of a glucose oxidase-gluconolactonase enzyme mixture has been found to increase substantially the ratio of gluconolactonase to glucose oxidase activities compared to the corresponding activity ratio for these enzymes in solution.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260201011
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  • 9
    Electronic Resource
    Electronic Resource
    Glucoamylase and glucose oxidase preparations and their combined application for conversion of maltose to gluconic acid (1977)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 19 (1977), S. 185-198 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The kinetic behavior of a system of multiple enzyme in solution has been studied in a variable volume batch reactor at pH 5, controlled dissolved oxygen concentration, and T = 30°C. The enzymes used were glucoamylase (R. delemar), glucose oxidase (A. niger), and gluconolactonase (A. niger), all of which are important commercial biocatalysts, and a disaccharide was employed as the starting substrate. This study includes the basic kinetic properties of individual enzymes and interactions between components of the reaction mixture. Classical Michaelis-Menten single substrate or two substrate kinetic with parameters based on initial rate data predict correctly the batch time course of the sequential reaction network.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260190203
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  • 10
    Electronic Resource
    Electronic Resource
    Analysis of fermentation processes using flow microflourometry: Single-parameter observations of batch bacterial growth (1979)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 21 (1979), S. 1995-2010 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The laser flow microfluorometer (FMF) can determine the amounts of certain components in single cells at sample rates of several thousand cells per second. This technique has been employed to characterize Bacillus subtilis populations in batch fermentations with different inocula. Protein and distributions obtained by FMF analyses at different times during the batch have been decomposed using an optimized fit of summed subpopulation distributions. The results of these decomposition calculations, some of which have been approximately confirmed by independent microscopic observations, indicate cells relative numbers of single rods, cell chains, spores, and swollen rounded cells change dramatically during the entire fermentation including the stationary phase. The dynamics of these subpopulations may be related to secondary metabolite production.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260211108
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