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  • 1
    Electronic Resource
    Electronic Resource
    Preparation and properties of Pb-doped Bi-Sr-Ca-Cu-O superconductors (1989)
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 66 (1989), S. 1881-1883 
    Details
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Notes: Electrical and magnetic properties of the superconducting oxides with nominal composition (Bi0.7 Pb0.3 )2Sr2Ca2 Cu3 Ox prepared from polymeric precursors have been investigated. Superconducting transition with zero-resistance temperature at T=108 K was achieved for a sample sintered at 840 °C under a low oxygen pressure. The critical current density at 77 K in a zero magnetic field is ∼400 A/cm2 , which is much higher than that of the Pb-free sample. Variations of the superconducting transition temperature, the critical current density, and magnetic properties with heat treatment time are discussed in connection with the structural properties.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.344370
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  • 2
    Electronic Resource
    Electronic Resource
    Annealing effects in ZnSe/GaAs heterostructure grown by molecular beam epitaxy (1997)
    Woodbury, NY : American Institute of Physics (AIP)
    Applied Physics Letters 71 (1997), S. 3257-3259 
    Details
    ISSN: 1077-3118
    Source: AIP Digital Archive
    Topics: Physics
    Notes: In the ZnSe/GaAs heterostructure, the problems of interdiffusion and thermal stability are very crucial. We have investigated the effects of annealing on ZnSe grown on GaAs by photoluminescence and double-crystal x-ray measurement. In order to investigate annealing effects of the ZnSe/GaAs heterostructure, we used 1.0-μm-thick and 0.2-μm-thick samples. Samples were annealed in the temperature range of 200–500 °C in an N2 ambient for 3 min using a face-to-face configuration with ZnSe epitaxial layer as a cap layer. In the annealing temperature above 450 °C, new emission peaks appeared in the range of 2.62–2.72 eV. The biaxial compressive strain due to lattice mismatch at the growth temperature is mostly relaxed at 400 °C, and the epilayer annealed at 500 °C has a biaxial tensile strain. © 1997 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.120307
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  • 3
    Electronic Resource
    Electronic Resource
    Annealing behavior of Ar ion irradiated Bi2Sr2Can-1CunO4+2n superlattice and intergrowth films (1996)
    Springer
    Journal of low temperature physics 105 (1996), S. 1295-1300 
    Details
    ISSN: 1573-7357
    Keywords: 74.76.Bz ; 74.72.Hs
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract Artificially layered Bi2Sr2Can−1CunO4+n films were synthesized by sequential sputter deposition of BiO, SrCu0.5O1.5 and CaCuO2 layers. Annealing behavior of these films which were irradiated by Ar ions was studied. Defect assisted improvement of their crystalline perfection is expected which might results in the improvement of the superconducting properties of these films. An artificial film, such as an intergrowth of 2223 and 2234 phases, and superstructure films of (2245)1(2201)1 and (2234)1(2212)1, were irradiated by Ar ions (150 keV, 2−10×1012 ions/cm2) and annealed at 730 °C. An improvement of superconducting transition temperatures were observed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00753879
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  • 4
    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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  • 5
    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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  • 6
    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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  • 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 glucoamylase and glucose oxidase in activated carbon: Effects of particle size and immobilization conditions on enzyme activity and effectiveness (1983)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 25 (1983), S. 1923-1935 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Glucoamylase and glucose oxidase have been immobilized on carbodiimide-treated activated carbon particles of various sizes. Loading data indicate nonuniform distribution of immobilized enzyme within the porous support particles. Catalysts with different enzyme loading and overall activities have been prepared by varying enzyme concentration in the immobilizing solution. Analysis of these results by a new method based entirely upon experimentally observable catalyst properties indicates that intrinsic catalytic activity is reduced by immobilization of both enzymes. Immobilized glucoamylase intrinsic activity decreases with increasing enzyme loading, and similar behavior is suggested by immobilized glucose oxidase data analysis. The overall activity data interpretation method should prove useful in other immobilized enzyme characterization research, especially in situations where the intraparticle distribution of immobilized enzyme is nonuniform and unknown.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260250803
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  • 9
    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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  • 10
    Electronic Resource
    Electronic Resource
    Immobilization of enzymes in porous supports: Effects of support-enzyme solution contacting (1984)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 26 (1984), S. 892-900 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Proteins have been immobilized in porous support particles held in a fixed-bed reactor through which protein solution is continuously circulated. Changing the recirculation flow rate alters the observed immobilization kinetics and the maximum enzyme loading which can be achieved for glucose oxidase and glucoamylase on carbodiimide-treated activated carbon and for glucoamylase immobilized on CNBr-Sepharose 4B. Direct microscopic examination of FITC-labelled protein in sectioned Sepharose particles and indirect activity-loading studies with activated carbon-enzyme conjugates all indicate that immobilized enzyme is increasingly localized near the outer surface of the support particles at larger recirculation flow rates. Restricted diffusion of enzymes may be implicated in this phenomenon. These contacting effects may be significant considerations in the scaleup of processes for protein impregnation in porous supports, since apparent activity and stability of the final preparation depend on internal protein distribution.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260260812
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