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  • 1
    Electronic Resource
    Electronic Resource
    Enzyme membrane based upon polyamide-6 for oil hydrolysis (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Applied Polymer Science 46 (1992), S. 749-755 
    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
    Notes: This work presents the preparation of the enzyme membrane based upon polyamide-6 (PA-6) destined for the hydrolysis of oils. The transport properties of the base PA-6 membranes, i.e., their porosity and permeability coefficients, as well as the mode of their modification, aimed at the chemical binding of lipase molecules have been estimated. © 1992 John Wiley & Sons, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/app.1992.070460501
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  • 2
    Electronic Resource
    Electronic Resource
    Enantioselective esterification of butanol-2 in an enzyme membrane reactor (1993)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 13 (1993), S. 177-183 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: The enzymatic esterification of octanoic acid with racemic butanol-2 was investigated. Esterifications of the acid were performed in a forced flow enzyme membrane reactor. The used membrane was prepared by a phase inversion process in polyamide-6 solution followed by the chemical immobilization of a lipase-catalyst.Influences of water content and pH were estimated. Their optimum values are equal to 0.5% w/w and pH 8. The reaction rate (at 303 K) of 5.1 × 10-5 mol/h·cm2 of the membrane area, and at least 85% enantiomeric excess in the produced ester mixture were obtained.The activity of immobilized lipase in the membrane process is about two times higher than that of the native lipase in the esterification performed in a tank reactor.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370130217
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  • 3
    Electronic Resource
    Electronic Resource
    Kinetics of olive oil hydrolysis in an enzyme membrane reactor. Bond graph network model of reactor performance (part 1) (1997)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 17 (1997), S. 161-176 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Hydrolyses of olive oil were performed in a reactor with lipase immobilized on a laboratory ultrafiltration poliamide-6 membrane. The reactor consisted of two circulating phases of olive oil and buffer solution. For the characterization of the reactor performance, a model of the hydrolysis process was developed. It was created by means of thermodynamic network representation of both the chemical processes and the transport of the reactants. According to an estimated bond graph network, the model is represented quantatively by a set of thirty-three differential equations representing the time derivatives of the particular species concentration. The parameters of the model were estimated based on experimental data and/or literature notations. Close agreement of numerical estimations of the product concentrations with experimental data was gained. The model enabled an extended analysis of the influence of different reaction parameters, enzyme inhibition and concentration of the reactants on reactor performance.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370170207
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  • 4
    Electronic Resource
    Electronic Resource
    Lipase-catalyzed kinetic resolution of (R,S)-1-phenylethyl propionate in an enzyme membrane reactor (1997)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 17 (1997), S. 253-263 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Enzymatic stereoselective hydrolysis of (R,S)-1-phenylethyl propionate was performed in a stirred tank and in a biphasic enzyme membrane reactor. Lipase from Pseudomonas sp. was proved to be a good enantioselective catalyst for this reaction. The enzyme was covalently immobilized in a porous polyamide membrane (flat sheet as well as hollow-fibres) via glutaraldehyde. An influence of membrane hydrophobicity on reactor performance was observed. Initial lipase activity and productivity in the processes were equal to 1.05 × 10-4, 1.3 × 10-5 and 1.0 × 10-5 mole/(h × mg of enzyme) in the case of native lipase, in the aromatic polyamide hydrophobic membrane reactor and in the hydrophilic polyamide-6 membrane reactor, respectively. The influence of some factors such as temperature, pH, buffer concentration, initial substrate concentration and addition of β-cyclodextrin derivatives on reaction rate and enantioselectivity was investigated and discussed. In the enzyme membrane reactor both organic and aqueous phases circulated countercurrently on both sides of the membrane. At a conversion degree of under 55-60%, pure enantiomer of the remaining ester (i.e. 〉 98%) was obtained.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370170310
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