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  • 1
    Electronic Resource
    Electronic Resource
    A study of the separation efficiency of the batch-type thermal diffusion column with an impermeable barrier inserted between the plates (1986)
    s.l. : American Chemical Society
    Industrial and engineering chemistry 25 (1986), S. 367-372 
    Details
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/i100023a011
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  • 2
    Electronic Resource
    Electronic Resource
    Asymptotic Nusselt numbers for Newtonian flow through a parallel-plate channel with recycle (1988)
    Springer
    Heat and mass transfer 23 (1988), S. 179-181 
    Details
    ISSN: 1432-1181
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Description / Table of Contents: Zusammenfassung In dieser Untersuchung wurden allgemeine Ausdrücke hergeleitet um die asymptotische Nusselt-Zahl für eine Newtonsche Strömung durch einen Kanal aus parallelen Platten mit Rückführung an den Enden berechnen zu können. Es wurden numerische Ergebnisse mit den Dicken-Verhältnissen, als Parameter für verschiedene Rückführungs-verhältnisse, erhalten. Eine Regressionsanalyse zeigt, daß die Ergebnisse wie folgt ausgedrückt werden können: log Nur0,83=0,3589 (logδ)2 -0,2925 (logδ) + 0,3348 fürR ≥ 3, 0,1 ≤δ ≤ 0,9; logNu=0,5982(logδ)2 +0,3755 × 10−2 (logδ) + 0,8342 fürR ≤ 10−2, 0,1 ≤δ ≤ 0,9.
    Notes: Abstract General expressions for evaluating the asymptotic Nusselt number for a Newtonian flow through a parallel-plate channel with recycle at the ends have been derived. Numerical results with the ratio of thicknessesΔ as a parameter for various recycle ratios are obtained. A regression analysis shows that the results can be expressed by log Nur0.83=0.3589 (logΔ)2 -0.2925 (logδ) + 0.3348 forR ≥ 3, 0.1 ≤δ ≤ 0.9; logNu=0.5982(logδ)2 +0.3755 × 10−2 (logδ) +0.8342 forR ≤ 10−2, 0.1 ≤δ ≤ 0.9.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01376551
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  • 3
    Electronic Resource
    Electronic Resource
    Recycle effects on heat and mass transfer through a parallel-plate channel (1987)
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 33 (1987), S. 1743-1746 
    Details
    ISSN: 0001-1541
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aic.690331020
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  • 4
    Electronic Resource
    Electronic Resource
    A study of separation efficiency in thermal diffusion columns with a permeable vertical barrier (1986)
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 32 (1986), S. 971-980 
    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 separation theory in thermal diffusion columns with a permeable vertical barrier has been derived by making use of the orthogonal expansion method. It is shown that the undesirable remixing effect can be effectively reduced and controlled by introducing a permeable vertical barrier. Considerable improvement in separation was obtained when the position of the barrier was carefully chosen.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aic.690320607
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  • 5
    Electronic Resource
    Electronic Resource
    Effect of solvent on enantioselective esterification of naproxen by lipase with trimethylsilyl methanol (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 43 (1994), S. 64-68 
    Details
    ISSN: 0006-3592
    Keywords: enantioselectivity ; Naproxen ; esterification ; lipase ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Improvement of stereoselective resolution of racemic Naproxen, 2-(6-methoxy-2-naphthyl)propionic acid, was attempted with esterifcation reaction by Candida cylindracea lipase. By carefully selecting the organic medium, a 72-time enhancement of yield of the desired S-ester was achieved. The optimal reaction temperature was approximately 53°C, and an alcohol concentration between 20 mM and 40 mM in an 80% (v/v) isooctane and 20% (v/v) toluene mixture was found. © 1994 John Wiley & Sons, Inc.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260430109
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  • 6
    Electronic Resource
    Electronic Resource
    Action of lipolytical enzymes in biphasic organic-aqueous systems: Dynamics of the irreversible Michaelis-Menten reaction (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 41 (1993), S. 603-611 
    Details
    ISSN: 0006-3592
    Keywords: dynamics of lipolytic enzymes ; modal analysis ; biphasic systems ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Through simple model analysis, the mass action kinetic model for lipolytic enzymes in biphasic aqueous-organic systems can be simplified using the quasi-steady state assumption (or the quasi-equilibrium state assumption) for the adsorbed enzyme E* or the enzyme-substrate complex E*S. Some parameter combinations leading to the above assumptions are derived confirmed by full numerical integration of the whole enzymatic process. The results may be classified into three categories: (1) the quasi-equilibrium state assumption for E*, (2) the quasi-steady state assumption for E*, and (3) the quasi-steady state assumption for E*S. Further simplification for both E* and E*S is also discussed. © 1993 Wiley & Sons, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260410602
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  • 7
    Electronic Resource
    Electronic Resource
    Surfactant enhancement of (S)-naproxen ester productivity from racemic naproxen by lipase in isooctane (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 51 (1996), S. 148-156 
    Details
    ISSN: 0006-3592
    Keywords: surfactant ; lipase ; Naproxen ; esterification ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: In the enantioselective esterification of racemic Naproxen with trimethylsilyl methanol in isooctane by Candida cylindracea lipase, improvements in (S)-naproxen ester productivity and enzyme selectivity were demonstrated by adding bis(2-ethylhexyl) sodium sulfosuccinate (AOT) as the best surfactant. The effect of water content on the enhancement of enzyme activity was elucidated from the reduced adsorption of surfactant molecules on the lipase. A competitive inhibition by the alcohol and a noncompetitive inhibition by the surfactant to the enzyme were found from the kinetic analysis. By using a two-phase extraction, a complete separation of the surfactant from the organic solution was obtained. © 1996 John Wiley & Sons, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Extraordinary enantiospecificity of lipase catalysis in organic media induced by purification and catalyst engineering (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 52 (1996), S. 296-300 
    Details
    ISSN: 0006-3592
    Keywords: enantioselective esterification ; lipase ; propionic acid ; catalysis ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A purified lipase preparation from Candida rugosa was compared to its crude counterpart in anhydrous and slightly hydrated hydrophobic organic solvents. The purified lipase preparation was less active than the crude enzyme in dry n-heptane, whereas the presence of small concentrations of added water dramatically activated the purified enzyme but not the crude enzyme. Thus, in the presence of as little as 0.25 μL/mL of added water in n-heptane, the purified enzyme is over 230-fold more active and 6-fold more enantioselective than the dry enzyme suspension in the esterification of racemic 2-(4-chlorophenoxy)propionic acid with n-butanol. The reactivity and selectivity of this biocatalyst, however, was affected by coalescence of the enzyme preparation suspended in the wet organic solvent. Engineering the biocatalyst environment by dissolving the purified lipase in aqueous buffer and then adding this solution to n-heptane resulted in a precipitated enzyme preparation with smaller particle sizes that did not coalesce severely. In the presence of 5 μL/mL of water added with the enzyme, this pretreatment resulted in an activation over the dry, purified enzyme preparation of over 1800-fold and nearly enantiospecific catalysis (E 〉 100). Hence, by simply modifying the way enzymes are hydrated, dramatic activation of catalytic competency can be achieved. © 1996 John Wiley & Sons, Inc.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Kinetics of enzymatic hydrolysis of olive oil in biphasic organic-aqueous systems (1991)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 38 (1991), S. 761-766 
    Details
    ISSN: 0006-3592
    Keywords: biphasic system ; lipase-catalyzed hydrolysis ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A theoretical model for the lipase-catalyzed hydrolysis of high-concentration olive in biphasic isooctane-aqueous systems has been proposed and confirmed by experiments. The enzymatic reaction of the Michaelis-Menten type that occurred at the interface between organic and aqueous phases was assumed in deriving the rate equations, from which the maximum reaction rate could be obtained by carefully adjusting the volume ratio between the two phases to the optimal value. Equilibrium conversions higher than 98% for 0.1 g/L olive oil in isooctane were attained for systems with volume ratios up to one. Fractions of lipase and lipase-substrate complex adsorbed at the interface increased and seemed to approach to asymptotic values asthe rotation speed of impeller increased. Activity of the lipase showed no apparent change between 26 and 37°C, but decrease rapidly with temperature above 43°C. The methodology presented in this work might be used to find kinetic parameters for reactor design and scaleup.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260380710
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  • 10
    Electronic Resource
    Electronic Resource
    Kinetics, mechanism, and time course analysis of lipase-catalyzed hydrolysis of high concentration olive oil in AOT-isooctane reversed micelles (1991)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 38 (1991), S. 206-211 
    Details
    ISSN: 0006-3592
    Keywords: reversed micelles ; lipase ; hydrolysis ; competitive product inhibition ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Candida rugosa lipase has been used to investigate the hydrolysis of high concentration olive oil in the AOT-isooctane reversed micellar system at Wo = 10, pH 7.1, and 37°C. Results from this work show the hydrolytic reaction obeys Michaelis-Menten kinetics up to the initial substrate concentration of 1.37M, with turnover number kcat and Michaelis constant KM of 67.1 μmol/min mg enzyme and 0.717M, respectively. A competitive inhibition by the main product, oleic acid, has been found with a dissociation constant KI for the complex EP* of 0.089M. The rate equation was further analyzed in the time course reaction and was found in agreement with the experimental results for lower substrate concentrations, up to 0.341M. Large deviation occurred at high substrate concentrations, which may be due to the effects of large consumption of water on kinetics, on the formation of glycerol, and on the deactivation of lipase in the hydrolysis reaction as well.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260380213
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