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  • Biochemistry and Biotechnology  (3)
  • Computational Chemistry and Molecular Modeling  (3)
  • 1985-1989  (6)
  • 1920-1924
  • 1
    Electronic Resource
    Electronic Resource
    Continuous production of maltotetraose using immobilized Pseudomonas stutzeri amylase (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 32 (1988), S. 669-676 
    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 continuous production process of maltotetraose was investigated by using immobilized maltotetraose (G4)- forming amylase (1,4-α-D-glucan maltotetraohydrolase, EC3.2.1.60) from Pseudomonas stutzeri adsorbed on a macroporous hydrophobic resin. The maximum reaction rate was obtained at 55°C and the activation energy of hydrolysis by immobilized G4-forming amylase was calculated to be 8.45 kcal/mol. The maltotetraose yield was greatly influenced by the flow rate of substrate solution, its concentration, and the immobilized enzyme activity. The newly defined factor “specific space velocity” was successfully introduced to normalize the operating parameters. Using this factor, the immobilized enzyme reactor then can be simulated and the operating dynamics can be determined.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260320512
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  • 2
    Electronic Resource
    Electronic Resource
    Stability of immobilized maltotetraose-forming amylase from Pseudomonas stutzeri (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 33 (1989), S. 845-855 
    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 stability of immobilized maltotetraose (G4)-forming amylase (1,4-α-D-glucan maltoteraohydrolase, EC 3.2.1.60) from Pseudomonas stutzeri was investigated in both batch and continous processes. The inactivation process of the immobilized enzyme seemed to obey first-order kinetics, and the immobilized enzyme became more stable when coexisting with 20-30 wt % substrate and calcium ions. From intensive studies on the operational stability in the continuous process, the apparent half-life of G4 productivity in a constant-flow system was mainly affected by the reaction temperature, substrate concentration, and initial immobilized enzyme activity. A new factor, immobilized enzyme stability factor fs, was proposed to evaluate the half-life of the immobilized enzyme system.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260330708
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  • 3
    Electronic Resource
    Electronic Resource
    Depolymerization of chondroitin C Sulfate by immobilized Proteus vulgaris cells (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 28 (1986), S. 1707-1712 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Chondroitinase ABC catalyzing the depolymerization of chondroitin sulfate was induced by incubating the Proteus vulgaris cells in a medium containing chondroitin C sulfate as an inducer. Incubation of P. vulgaris cells for 12 h in the presence of 0.3% inducer was optimal to obtain the cells with highly active chondroitinase ABC. Such cells were immobilized in k-carrageenan gel lattice, and some properties of chondroitinase ABC in immobilized cells were studied in comparison with those of the enzyme without immobilization (free enzyme). The stabilities of the enzyme toward heat and storage were remarkably improved by immobilizing the cells in k-carrageenan gel lattice. Optimal pH and temperature for activity of the enzyme were slightly shifted to the alkaline region and higher temperature by immobilization and were 9.0 and 35°C, respectively.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260281114
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  • 4
    Electronic Resource
    Electronic Resource
    Theory of electron degradation and yields of initial molecular species produced by ionizing radiation (1987)
    New York, NY : Wiley-Blackwell
    International Journal of Quantum Chemistry 32 (1987), S. 251-266 
    Details
    ISSN: 0020-7608
    Keywords: Computational Chemistry and Molecular Modeling ; Atomic, Molecular and Optical Physics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Ionizing radiations generate in matter a large number of energetic electrons, which in turn collide with molecules in matter, produce ions and excited states, and thereby degrade in energy. The description of the consequences of many collision processes to the electrons and to matter is the goal of the electron degradation theory. We summarize the current understanding of this topic, which is important as a basis of radiation chemistry and biology. In addition, we present an initial report of our new work, namely, a generalization of the Spencer-Fano theory to time-dependent cases.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/qua.560320728
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  • 5
    Electronic Resource
    Electronic Resource
    Experimental and theoretical studies of small-angle electron scattering by the water molecule (1986)
    New York, NY : Wiley-Blackwell
    International Journal of Quantum Chemistry 30 (1986), S. 821-830 
    Details
    ISSN: 0020-7608
    Keywords: Computational Chemistry and Molecular Modeling ; Atomic, Molecular and Optical Physics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The total (elastic plus inelastic) intensities of 51 keV electrons scattered by water molecules have been measured over a range of 1 ≦ K = (4π/λ) sin(θ/2) ≦ 12 Å-1. A computer program, ELIC, has been written for calculating the total intensities of electrons scattered by free molecules. The intensities can be calculated with self-consistent field and configuration interaction wavefunctions. The theoretical intensities based on a CI wavefunction are in good agreement with the observed intensities.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/qua.560300611
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  • 6
    Electronic Resource
    Electronic Resource
    Application of the higher order finite-element method to one-dimensional Schrödinger equation (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Computational Chemistry 9 (1988), S. 827-835 
    Details
    ISSN: 0192-8651
    Keywords: Computational Chemistry and Molecular Modeling ; Biochemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Computer Science
    Notes: The accuracy and applicability of the finite-element method of the higher order interpolation functions to the one-dimensional Schrödinger equation were examined. When the fifth-order Lagrange and Hermite interpolation functions were used as the basis functions, practically exact solutions were obtained for all eigenvalues of several model potential energy functions. It was demonstrated that the appropriate analytical integration over the potential energy function within each element is important in the matrix element evaluation. The accuracy of the method was examined for the potential functions with a double minimum, which has a large classically forbidden region. The method was also applied to evaluate the Franck-Condon factors of the transitions between the 1 1Σg+ and 2 1Σu+ states of Na2; the latter state having a double minimum in its potential energy function.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcc.540090805
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