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  • Articles: DFG German National Licenses  (90)
  • Chemistry  (90)
  • fluorescence  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Densities of amorphous polymers at high pressures (1974)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Applied Polymer Science 18 (1974), S. 3779-3781 
    Details
    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
    Additional Material: 3 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/app.1974.070181224
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  • 2
    Electronic Resource
    Electronic Resource
    Thermodynamics of phase equilibria in aqueous-organic systems with salt (1994)
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 40 (1994), S. 676-691 
    Details
    ISSN: 0001-1541
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A semiempirical thermodynamic method is developed to establish a framework for calculating vapor-liquid and liquid-liquid equilibria in ternary systems containing water, an organic solvent, and a salt. Careful attention is given to precise definition of standard states. Short-range ion-solvent forces are taken into account primarily by a chemical-equilibrium method based on stepwise ion solvation; however, physical contributions also contribute. Water-cosolvent nonideality is described by an extended equation of the van Laar form. Long-range electrostatic forces between ions are taken into account by an extended Debye-Hückel equation with corrections for transferring from a McMillan-Mayer to a Lewis-Randall framework.The new method is illustrated with results for several systems including saturated aqueous mixtures of LiBr or LiCl with methanol where the salt concentration exceeds 20 molal. The method developed here is of particular interest for process calculations in extractive crystallization, a low-energy operation for producing salt from aqueous solution.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aic.690400411
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  • 3
    Electronic Resource
    Electronic Resource
    Extractive bioconversions in aqueous two-phase systems: Enzymatic hydrolysis of casein proteins (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 40 (1992), S. 195-206 
    Details
    ISSN: 0006-3592
    Keywords: bioconversions ; hydrolysis ; casein proteins ; catalysis ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Partition coefficients in poly(ethylene glycol)/dextran aqueous two-phase systems are reported for mixed-casein and its components, α, β and κ casein. Rates of casein proteolysis by α-chymotrypsin and by trypsin are reported in single-phase and aqueous two-phase reactor systems. The advantages resulting from selective partitioning of substrates, enzymes, and products are examined in terms of relative volumetric reaction rates.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260400202
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  • 4
    Electronic Resource
    Electronic Resource
    The effect of aqueous surfactant solutions on alcohol dehydrogenase (LADH) (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 41 (1993), S. 156-161 
    Details
    ISSN: 0006-3592
    Keywords: LADH ; surfactants ; ERP ; CD ; fluorescence ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Alcohol dehydrogenase (LADH) was studied in aqueous solutions of surfactants to determine its structural and catalytic characteristics. Fluorescence, circular dichroism (CD), and electron paramagnetic resonance (ERP) techniques were used to study structural changes to the enzyme. The activity of LADH in catalyzing the oxidation of ethanol was investigated. Short-chain alkyl sulfonates and sulfates did not deactivate LADH or alter its structure. Longer and branched alkyl sulfates and sulfonates, as well as a cationic surfactant (CTAB), affected both LADH activity and conformation. © 1993 John Wiley & Sons, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260410120
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  • 5
    Electronic Resource
    Electronic Resource
    Liquid-liquid phase separations in aqueous solutions of globular proteins (1993)
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 39 (1993), S. 215-223 
    Details
    ISSN: 0001-1541
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A simple statistical-mechanical theory, known as the random-phase approximation, is applied to study liquid-liquid phase separations in solutions of globular proteins. Phase separation may be induced by addition of nonionic polymer or/and ordinary electrolytes. In this analysis, the osmotic-attraction mechanism, whereby the depletion of “solvent” particles between two proteins causes an attractive force, is primarily responsible for phase separation. For one-component models of protein solutions, the theory yields simple algebraic expressions for the equation of state and for the chemical potential of the protein. This analytical theory describes the observed solubility behavior of proteins, including the effect of protein and polymer size, protein charge and concentration, and concentration of simple electrolytes.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aic.690390204
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  • 6
    Electronic Resource
    Electronic Resource
    Salting out of aqueous proteins: Phase equilibria and intermolecular potentials (1995)
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 41 (1995), S. 996-1004 
    Details
    ISSN: 0001-1541
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Salting-out phase equilibria are reported for lysozyme and α-chymotrypsin from concentrated ammonium-sulfate solutions. Supernatant and dense-phase protein concentrations and the resulting protein partition coefficients are given as a function of solution pH and ionic strength. Phase equilibria with a trivalent salt (sodium citrate) confirm that ionic strength, rather than salt concentration, is the appropriate variable describing phase equilibria. The salting-out behavior of a mixture of an aqueous lysozyme and α-chymotrypsin is independent of the presence of the other protein.Parameters for a molecular-thermodynamic description of salting-out behavior are obtained from low-angle laser-light scattering (LALLS). Osmotic second virial coefficients from LALLS are reported over a range of pH for dilute chymotrypsin concentrations in aqueous electrolyte solutions at 0.01 and 1.0 M ionic strengths. Effective Hamaker constants, regressed from experimental osmotic second virial coefficients, are determined for models of the protein - protein potential of mean force. In addition to excluded volume, dispersion, and shielded charge - charge potentials, the description of protein - protein interactions includes attractive charge - dipole and dipole - dipole potentials as well as an osmotic-attraction potential that becomes important at high salt concentrations. Protein dipole - dipole potentials are required to account for the observed pH dependence of osmotic second virial coefficients, especially at low ionic strength.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aic.690410430
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  • 7
    Electronic Resource
    Electronic Resource
    Letters to the editor (1997)
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 43 (1997), S. 1372-1374 
    Details
    ISSN: 0001-1541
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aic.690430529
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  • 8
    Electronic Resource
    Electronic Resource
    Mechanisms of protein solubilization in reverse micelles (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 40 (1992), S. 91-102 
    Details
    ISSN: 0006-3592
    Keywords: reverse micelle ; solubilization ; light scattering ; chymotrypsin ; LADH ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Solubilization properties of α-chymotrypsin and alcohol dehydrogenase (LADH) in reverse micelles are reported for three different solubilization techniques. The solubilization properties for these two proteins depend on the method used for protein addition. The addition of a dry protein powder to a reverse-micelle-containing organic phase does not appreciably solubilize the protein until the diameter of the reverse micelle is similar to that of the protein. However, when an aqueous protein solution is injected an organic phase, protein solubilization is not strongly dependent on micelle size. For chymotrypsin, multiple protein occupancy occurs at large micelle size, with as many as 11 chymotrypsin molecules solubilized in one reverse micelle. The solubilization of chymotrypsin using a phase-transter technique with a positively charged surfactant follows the expected traned based on protein-surfactant electrostatic interactions. When a negatively charged sufactants is used for phase transfer, at low pH the solubilization data do not fit this electrostatic interaction mechanism. In this case, proteinsurfactant aggregation may be occurring at the aqueousorganic interface.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260400114
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  • 9
    Electronic Resource
    Electronic Resource
    Application of integral-equation theory to aqueous two-phase partitioning systems (1993)
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 39 (1993), S. 1539-1557 
    Details
    ISSN: 0001-1541
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A molecular-thermodynamic model is developed for representing thermodynamic properties of aqueous two-phase systems containing polymers, electrolytes, and proteins. The model is based on McMillan-Mayer solution theory and the generalized mean-spherical approximation to account for electrostatic forces between unlike ions. The Boublik-Mansoori equation of state for hard-sphere mixtures is coupled with the osmotic virial expansion truncated after the second-virial terms to account for short-range forces between molecules.Osmotic second virial coefficients are reported from low-angle laser-light scattering (LALLS) data for binary and ternary aqueous solutions containing polymers and proteins. Ion-polymer specific-interaction coefficients are determined from osmoticpressure data for aqueous solutions containing a water-soluble polymer and an alkali chloride, phosphate or sulfate salt.When coupled with LALLS and osmotic-pressure data reported here, the model is used to predict liquid-liquid equilibria, protein partition coefficients, and electrostatic potentials between phases for both polymer-polymer and polymer-salt aqueous two-phase systems. For bovine serum albumin, lysozyme, and α-chymotrypsin, predicted partition coefficients are in excellent agreement with experiment.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aic.690390913
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  • 10
    Electronic Resource
    Electronic Resource
    Electrostatic potentials and protein partitioning in aqueous two-phase systems (1991)
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 37 (1991), S. 1401-1409 
    Details
    ISSN: 0001-1541
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A thermodynamic analysis unambiguously relates interfacial-electrostatic-potential differences measured with Ag/AgCl capillary electrodes to the equilibrium properties of an aqueous two-phase system. Interfacial electrostatic potentials were measured as a function of total α-cyclodextrin concentration in an aqueous two-phase system containing 9.1 wt. % poly (ethylene glycol), 6.1 wt. % Dextran T-70, and 1-mM potassium iodide. An order-of-magnitude increase in the interfacial electrostatic potential was observed as the total concentration of α-cyclodextrin increased from 0 to 1 mM. Measured partition coefficients for α-chymotrypsin, lysozyme, and bovine serum albumin depend strongly on α-cyclodextrin concentration. For example, as the concentration of α-cyclodextrin rises from 0 to 1 mM, the partition coefficient of lysozyme decreases from 1.7 to 0.55. These measurements are in good agreement with theoretical expectations.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aic.690370912
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