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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 42 (1993), S. 765-771 
    ISSN: 0006-3592
    Keywords: lipolysis ; lipases ; reversed micelles ; modeling ; second-order model ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Olive oil hydrolysis using Chromobacterium viscosum lipase B in a reversed micellar media was investigated in a membrane reactor. The dynamic evolution of the product concentration both in the concentrate and permeate stream was analyzed using a mechanistic model previously developed by us and further modified in this work. A kinetic law with a second-order dependence in the substrate concentration and nonlinear product inhibition was found to be the most adequate for the description of the hydrolysis data over an extensive range of time and substrate concentration. These findings are discussed in terms of the specific interactions occurring in the membrane reactor. © 1993 John Wiley & Sons, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 38 (1991), S. 1302-1307 
    ISSN: 0006-3592
    Keywords: liquid-liquid extraction ; selective separation of proteins ; reversed micelles ; purification ; lipases ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Selective separation and purification of two lipases form Chromobacterium viscosum were carried out by liquid-liquid extraction using a reversed micellar system. Optimum parameters for extraction were determined using a 250 mM AOT micellar solution in isooctane. Complete separation of the two lipases was achieved at pH 6.0 with a 50mM potassium phosphate buffer solution containing 50 mM KCI. By adding 2.5% by volume of ethanol to the lipase-loaded micellar solution, 85% of the extracted lipase could be recovered in a new aqueous phase, 50 mM K2HPO4 with 50 mM KCl, at pH 9.0. Lipase A was purified 2.6-fold with a recovery of 86%, and lipase B by 1.5-fold with a recovery of 76%.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 41 (1993), S. 761-770 
    ISSN: 0006-3592
    Keywords: ultrafiltration membrane bioreactor ; reversed micelles ; lipase ; product separation ; lipolysis ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The enzymatic hydrolysis of olive oil using Chromobacterium viscosum lipase B encapsulated in reversed micelles of dioctyl sodium sulfosuccinate (AOT) in isooctane was investigated in an ultrafiltration ceramic membrane reactor of tubular type, operating in a batch mode. Water concentration was found to be a critical parameter in the enzyme kinetics and hydrolysis yield of the reaction. The size of micelles, recirculation rate, and substrate concentration were found to be the major factors affecting the separation process. A correlation that enables the prediction of final conversion degrees in this bioreactor from the initial reaction conditions was established. © 1993 Wiley & Sons, Inc.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 42 (1993), S. 326-332 
    ISSN: 0006-3592
    Keywords: lipolytic enzymes ; cutinases ; ester synthesis ; stability ; reversed micelles ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Fusarium solani pisi recombinant cutinase, solubilized in AOT/isooctane-reversed micelles, was used to catalyze the esterification of fatty acids with aliphatic alcohols. Some relevant parameters for the enzyme activity such as pH, Wo (water/surfactant molar ratio), temperature, and substrate concentration were optimized. Maximal specific activity was obtained for hexanol. The cutinase showed selectivity for short-chain fatty acids. The stability of the microencapsulated cutinase was investigated at various concentrations of water and different values of pH. Oleic acid had a negative effect on the cutinase stability, while hexanol proved to be a strong stabilizer increasing the half-life of the enzyme about 45 times. © 1993 John Wiley & Sons, Inc.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 42 (1993), S. 759-764 
    ISSN: 0006-3592
    Keywords: Lipolysis ; modeling ; lipases ; reversed micelles ; fatty acid inhibition ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Triglyceride hydrolysis using Chromobacterium viscosum lipase B in a reversed micellar media was investigated in a batch-type reactor. The dynamic evolution of the product concentration was analyzed using several mechanistic models, both from the literature and developed in this work. A kinetic model with nonlinear product inhibition was found to be the most adequate for the description of batch hydrolysis data over an extensive range of time and substrate concentration. The obtained rate equation described the time course of not only the reactions performed in this work, at different water contents (W0 = 7, 24) and pH values, but also the experimental results obtained in the literature with a Candida rugosa lipase. © 1993 John Wiley & Sons, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Chichester : Wiley-Blackwell
    Journal of Chemical Technology AND Biotechnology 63 (1995), S. 181-189 
    ISSN: 0268-2575
    Keywords: phospholipase A2 ; reversed micelles ; lecithin hydrolysis ; lysophospholipids ; free fatty acids ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: The hydrolysis of egg yolk lecithin was studied as catalysed by porcine pancreatic phospholipase A2 (phosphatide 2-acyl-hydrolase, EC 3.1.1.4) entrapped in reversed micelles of lecithin and sodium dioctyl sulphosuccinate (AOT) in isooctane. The influence of relevant parameters such as temperature, pH, water content, and buffer, AOT, lecithin, calcium and enzyme concentrations was investigated. The order in which the reactants were mixed showed a strong influence on catalytic activity. Higher activities were obtained if the enzyme, water and calcium were first solubilized and pre-equilibrated in plain AOT reversed micelles before the addition of the substrate. Maximum activity was obtained at 750 mmol dm-3 calcium in the water pool of the micelles, which is an extremely high concentration when compared with the values reported in the literature. This was related to the formation of divalent chelates of calcium with AOT that compete with the binding of the co-factor to the enzyme. Accordingly, the optimum concentration of calcium in the inner core of the micelles decreased from 750 to 500 mmol dm-3 when the AOT concentration was lowered from 15 to 10 mmol dm-3.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
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