Details
| Original language | English |
|---|---|
| Pages (from-to) | B31-B37 |
| Journal | The Chemical Engineering Journal |
| Volume | 29 |
| Issue number | 2 |
| Publication status | Published - Oct 1984 |
Abstract
Only a few methods are known for the continuous production of L isomers using racemic mixtures of amino acids. A new method has been developed which uses α-chymotrypsin (E.C.3.4.21.1) immobilized in a liquid surfactant membrane emulsion. This enzyme converts DL-phenylalanine methyl ester to L-phenylalanine and D-ester. The aqueous enzyme solution was immobilized in a suitable membrane phase (kerosene or cyclohexane using Span 80 as an emulsifier). The loss of enzyme activity was examined for various membrane compositions. The substrate permeates the organic phase, and therefore a quaternary ammonium salt (Adogen 464) is needed as a carrier to transport the L-amino acid from the inner enzyme phase through the organic membrane phase. The optimum reaction conditions are 25 °C and pH 6; the activity loss is about 70%. Conversion data were calculated for continuous amino acid production by means of a simple two-parameter (Vmax and Ks) model and were compared with experimental results. The predicted conversions were slightly higher than the values obtained by experiment.
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In: The Chemical Engineering Journal, Vol. 29, No. 2, 10.1984, p. B31-B37.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Production of L-amino acid by continuous enzymatic hydrolysis of DL-amino acid methyl ester by the liquid membrane technique
AU - Scheper, Th
AU - Halwachs, W.
AU - Schügerl, K.
PY - 1984/10
Y1 - 1984/10
N2 - Only a few methods are known for the continuous production of L isomers using racemic mixtures of amino acids. A new method has been developed which uses α-chymotrypsin (E.C.3.4.21.1) immobilized in a liquid surfactant membrane emulsion. This enzyme converts DL-phenylalanine methyl ester to L-phenylalanine and D-ester. The aqueous enzyme solution was immobilized in a suitable membrane phase (kerosene or cyclohexane using Span 80 as an emulsifier). The loss of enzyme activity was examined for various membrane compositions. The substrate permeates the organic phase, and therefore a quaternary ammonium salt (Adogen 464) is needed as a carrier to transport the L-amino acid from the inner enzyme phase through the organic membrane phase. The optimum reaction conditions are 25 °C and pH 6; the activity loss is about 70%. Conversion data were calculated for continuous amino acid production by means of a simple two-parameter (Vmax and Ks) model and were compared with experimental results. The predicted conversions were slightly higher than the values obtained by experiment.
AB - Only a few methods are known for the continuous production of L isomers using racemic mixtures of amino acids. A new method has been developed which uses α-chymotrypsin (E.C.3.4.21.1) immobilized in a liquid surfactant membrane emulsion. This enzyme converts DL-phenylalanine methyl ester to L-phenylalanine and D-ester. The aqueous enzyme solution was immobilized in a suitable membrane phase (kerosene or cyclohexane using Span 80 as an emulsifier). The loss of enzyme activity was examined for various membrane compositions. The substrate permeates the organic phase, and therefore a quaternary ammonium salt (Adogen 464) is needed as a carrier to transport the L-amino acid from the inner enzyme phase through the organic membrane phase. The optimum reaction conditions are 25 °C and pH 6; the activity loss is about 70%. Conversion data were calculated for continuous amino acid production by means of a simple two-parameter (Vmax and Ks) model and were compared with experimental results. The predicted conversions were slightly higher than the values obtained by experiment.
UR - http://www.scopus.com/inward/record.url?scp=0021507424&partnerID=8YFLogxK
U2 - 10.1016/0300-9467(84)85036-4
DO - 10.1016/0300-9467(84)85036-4
M3 - Article
AN - SCOPUS:0021507424
VL - 29
SP - B31-B37
JO - The Chemical Engineering Journal
JF - The Chemical Engineering Journal
SN - 0300-9467
IS - 2
ER -