Details
| Original language | English |
|---|---|
| Pages (from-to) | 345-350 |
| Number of pages | 6 |
| Journal | German Chemical Engineering |
| Volume | 8 |
| Issue number | 6 |
| Publication status | Published - 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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In: German Chemical Engineering, Vol. 8, No. 6, 11.1985, p. 345-350.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - ENZYMATIC PRODUCTION OF L-AMINO ACID WITH CONTINUOUS COENZYME REGENERATION BY LIQUID MEMBRANE TECHNIQUE.
AU - Makryaleas, Kyriakos
AU - Scheper, Thomas
AU - Schuegerl, Karl
AU - Kula, Maria Regina
PY - 1985/11
Y1 - 1985/11
N2 - 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.
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.
UR - http://www.scopus.com/inward/record.url?scp=0022151621&partnerID=8YFLogxK
M3 - Article
AN - SCOPUS:0022151621
VL - 8
SP - 345
EP - 350
JO - German Chemical Engineering
JF - German Chemical Engineering
SN - 0343-5539
IS - 6
ER -