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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    The @journal of physical chemistry 〈Washington, DC〉 97 (1993), S. 13180-13191 
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Physical Chemistry 49 (1998), S. 99-123 
    ISSN: 0066-426X
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Chemistry and Pharmacology , Physics
    Notes: Abstract Chemical reaction and optical dynamics in the liquid phase are strongly affected by specific solute-solvent interactions. The dynamical part of this coupling leads to energy fluctuations. The associated energy gap dynamics can be probed by using various nonlinear optical spectroscopies. We discuss various forms of photon echo-time-integrated, time-gated, and heterodyne-detected photon echo-as well as Fourier transform spectral interferometry. It is shown that for solutions of the dye molecule DTTCI, a system-bath correlation function can be acquired that provides a quantitative description of all (non)linear spectroscopic experiments. The deduced correlation function is projected onto the multimode Brownian oscillator model, which allows for a physical interpretation of the multiple-time correlation function and a determination of the spectral density relevant to the solvation process. The following applications of photon echo to condensed phase dynamics are discussed: enhanced vibrational mode suppression, Liouville pathways interference, and dynamical Stokes shift. Recent results of echo-peak shift experiments on the hydrated electron are also presented. The review concludes that photon echo should be useful as a novel tool to explore transition state dynamics.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 105 (1996), S. 2953-2960 
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: It is demonstrated that enhanced mode suppression in stimulated photon echo experiments can be obtained by diagonal time gating of the echo. This technique is especially important when the optical dynamics of the system is non-Markovian. A two-mode Brownian oscillator model is used to analyze the effect of time gating on the stimulated photon echo. The method is demonstrated on a dye solution of DTTCI in ethylene glycol at room temperature. Experimentally, time gating of the echo is accomplished by means of femtosecond phase-locked heterodyne detected stimulated photon echo. The vibrational dynamics in this system are explored by conventional stimulated photon echo experiments. Especially stimulated photon echo-maximum shift measurements are found to be particularly useful. © 1996 American Institute of Physics.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Colloid & polymer science 257 (1979), S. 1203-1206 
    ISSN: 1435-1536
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Summary The copolymerization of N,N-diethylacrylamide (Ml) with methyl acrylate (M2) was investigated and reactivity ratiosr 1= 0.41 andr 2 = 0.52 obtained. Also the distribution of diad fractions was calculated and the results were interpreted in terms of the product of reactivity ratios. The tendency of the two monomers to alternate was explained on the basis of differences in polatities between the double bonds, this explanation being supported both by the values ofe parameter and NMR spectroscopy data. A copolymerization mechanism was suggested.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 12 (1992), S. 497-507 
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: The paper deals with the pectolytic enzymes immobilization on different acrylic supports, and the application of immobilized preparations in the apple juice pectinization process.The correlation between the protein content (Cp) and specific catalytic activities of immobilized enyzme preparations suggest a specific immobilization process only in the case of PONILEX ASH type acrylic supports.The active immobilization degree on PONILEX ASH type supports of Ultrazym 100 G and technical pectinase extract ranged from 99.80 to 296.40% for the Pectinesterase (PE) activity, and from 101.85 to 252.94% for the chain splitting (CS) activity, proving that the ionic immobilization process is a selective one. The simulated operational stability of the immobilized pectolytic enzymes tested by the PE and CS activity values proves the preservation of enzyme catalytic activity.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 14 (1994), S. 75-86 
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: This paper deals with the study of the behaviour of Amyloglucosidase covalently immobilized on acrylic supports in the maltodextrin hydrolysis process. The specific catalytic activity of the different immobilized Amyloglucosidase preparations critically depends on their protein content. The maltodextrin hydrolysis in the presence of the immobilized Amyloglusidase is a diffusion-controlled process. The simulated operational stability of the immobilized Amyloglucosidase tested by the specific activity and the substrate conversion proves the conservation of the catalytic enzymatic activity.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
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