ENZYMATIC PRODUCTION OF L-AMINO ACID WITH CONTINUOUS COENZYME REGENERATION BY LIQUID MEMBRANE TECHNIQUE.

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Original languageEnglish
Pages (from-to)345-350
Number of pages6
JournalGerman Chemical Engineering
Volume8
Issue number6
Publication statusPublished - Nov 1985

Abstract

L-Leucine-dehydrogenase (LEUDH) catalyzes the reductive amination of alpha -ketoisocaproate to L-leucine. During this reaction, NADH is oxidized and simultaneously reduced by formatedehydrogenase (FDH). The two enzymes and the coenzyme were immobilized in a liquid membrane emulsion. Several organic phases and emulsifiers were tested, in order to obtain suitable immobilization systems. Batch tests were carried out for optimization of operating conditions and determination of kinetic parameters. Mass transfer through the membrane is the rate determining step. Permeation coefficients for the substrates and product were determined on solid-supported liquid membranes.

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ENZYMATIC PRODUCTION OF L-AMINO ACID WITH CONTINUOUS COENZYME REGENERATION BY LIQUID MEMBRANE TECHNIQUE. / Makryaleas, Kyriakos; Scheper, Thomas; Schuegerl, Karl et al.
In: German Chemical Engineering, Vol. 8, No. 6, 11.1985, p. 345-350.

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title = "ENZYMATIC PRODUCTION OF L-AMINO ACID WITH CONTINUOUS COENZYME REGENERATION BY LIQUID MEMBRANE TECHNIQUE.",
abstract = "L-Leucine-dehydrogenase (LEUDH) catalyzes the reductive amination of alpha -ketoisocaproate to L-leucine. During this reaction, NADH is oxidized and simultaneously reduced by formatedehydrogenase (FDH). The two enzymes and the coenzyme were immobilized in a liquid membrane emulsion. Several organic phases and emulsifiers were tested, in order to obtain suitable immobilization systems. Batch tests were carried out for optimization of operating conditions and determination of kinetic parameters. Mass transfer through the membrane is the rate determining step. Permeation coefficients for the substrates and product were determined on solid-supported liquid membranes.",
author = "Kyriakos Makryaleas and Thomas Scheper and Karl Schuegerl and Kula, {Maria Regina}",
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volume = "8",
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journal = "German Chemical Engineering",
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AU - Makryaleas, Kyriakos

AU - Scheper, Thomas

AU - Schuegerl, Karl

AU - Kula, Maria Regina

PY - 1985/11

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AB - L-Leucine-dehydrogenase (LEUDH) catalyzes the reductive amination of alpha -ketoisocaproate to L-leucine. During this reaction, NADH is oxidized and simultaneously reduced by formatedehydrogenase (FDH). The two enzymes and the coenzyme were immobilized in a liquid membrane emulsion. Several organic phases and emulsifiers were tested, in order to obtain suitable immobilization systems. Batch tests were carried out for optimization of operating conditions and determination of kinetic parameters. Mass transfer through the membrane is the rate determining step. Permeation coefficients for the substrates and product were determined on solid-supported liquid membranes.

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JF - German Chemical Engineering

SN - 0343-5539

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