Production of L-amino acid by continuous enzymatic hydrolysis of DL-amino acid methyl ester by the liquid membrane technique

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OriginalspracheEnglisch
Seiten (von - bis)B31-B37
FachzeitschriftThe Chemical Engineering Journal
Jahrgang29
Ausgabenummer2
PublikationsstatusVeröffentlicht - Okt. 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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Production of L-amino acid by continuous enzymatic hydrolysis of DL-amino acid methyl ester by the liquid membrane technique. / Scheper, Th; Halwachs, W.; Schügerl, K.
in: The Chemical Engineering Journal, Jahrgang 29, Nr. 2, 10.1984, S. B31-B37.

Publikation: Beitrag in FachzeitschriftArtikelForschungPeer-Review

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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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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.

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