Production of optically pure L-valine in fluidized and packed bed reactors with immobilized L-aminoacylase

A process to obtain L‐valine has been developed using fluidized and packed bed reactors with L‐aminoacylase (from hog kidney) immobilized by covalent binding. L‐Valine production using the immobilized derivative of L‐aminoacylase in fluidized and packed bed reactors was studied at three different su...

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Veröffentlicht in:Journal of chemical technology and biotechnology (1986) 1999-05, Vol.74 (5), p.403-408
Hauptverfasser: Bódalo-Santoyo, A, Gómez-Carrasco, J L, Gómez-Gómez, E, Bastida-Rodriquez, J, Máximo-Martín, M F, Hidalgo-Montesinos, A M
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container_issue 5
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container_title Journal of chemical technology and biotechnology (1986)
container_volume 74
creator Bódalo-Santoyo, A
Gómez-Carrasco, J L
Gómez-Gómez, E
Bastida-Rodriquez, J
Máximo-Martín, M F
Hidalgo-Montesinos, A M
description A process to obtain L‐valine has been developed using fluidized and packed bed reactors with L‐aminoacylase (from hog kidney) immobilized by covalent binding. L‐Valine production using the immobilized derivative of L‐aminoacylase in fluidized and packed bed reactors was studied at three different substrate concentrations and two different flow rates. Higher productions were obtained in the packed bed reactor in all cases. The different solubilities of L‐valine and acetyl‐D‐valine in ethanol were used to purify L‐amino acid from the reactor effluents. The amount of added ethanol did not influence the separation yields, although the purity of L‐valine was strongly affected by this parameter. The last step involved was racemization of the unhydrolyzed acetyl‐D‐valine, which was then used as substrate in a new reaction cycle. © 1999 Society of Chemical Industry
doi_str_mv 10.1002/(SICI)1097-4660(199905)74:5<403::AID-JCTB51>3.0.CO;2-N
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L‐Valine production using the immobilized derivative of L‐aminoacylase in fluidized and packed bed reactors was studied at three different substrate concentrations and two different flow rates. Higher productions were obtained in the packed bed reactor in all cases. The different solubilities of L‐valine and acetyl‐D‐valine in ethanol were used to purify L‐amino acid from the reactor effluents. The amount of added ethanol did not influence the separation yields, although the purity of L‐valine was strongly affected by this parameter. 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Chem. Technol. Biotechnol</addtitle><description>A process to obtain L‐valine has been developed using fluidized and packed bed reactors with L‐aminoacylase (from hog kidney) immobilized by covalent binding. L‐Valine production using the immobilized derivative of L‐aminoacylase in fluidized and packed bed reactors was studied at three different substrate concentrations and two different flow rates. Higher productions were obtained in the packed bed reactor in all cases. The different solubilities of L‐valine and acetyl‐D‐valine in ethanol were used to purify L‐amino acid from the reactor effluents. The amount of added ethanol did not influence the separation yields, although the purity of L‐valine was strongly affected by this parameter. The last step involved was racemization of the unhydrolyzed acetyl‐D‐valine, which was then used as substrate in a new reaction cycle. © 1999 Society of Chemical Industry</description><subject>Amino acids</subject><subject>Bioconversions. Hemisynthesis</subject><subject>Biological and medical sciences</subject><subject>Bioreactors</subject><subject>Biotechnology</subject><subject>Chemical bonds</subject><subject>Ethanol</subject><subject>fluidized</subject><subject>Fluidized beds</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>immobilized enzyme</subject><subject>L-aminoacylase</subject><subject>L-valine</subject><subject>Methods. Procedures. 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Chem. Technol. Biotechnol</addtitle><date>1999-05</date><risdate>1999</risdate><volume>74</volume><issue>5</issue><spage>403</spage><epage>408</epage><pages>403-408</pages><issn>0268-2575</issn><eissn>1097-4660</eissn><coden>JCTBDC</coden><abstract>A process to obtain L‐valine has been developed using fluidized and packed bed reactors with L‐aminoacylase (from hog kidney) immobilized by covalent binding. L‐Valine production using the immobilized derivative of L‐aminoacylase in fluidized and packed bed reactors was studied at three different substrate concentrations and two different flow rates. Higher productions were obtained in the packed bed reactor in all cases. The different solubilities of L‐valine and acetyl‐D‐valine in ethanol were used to purify L‐amino acid from the reactor effluents. The amount of added ethanol did not influence the separation yields, although the purity of L‐valine was strongly affected by this parameter. 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1097-4660
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source Wiley Online Library Journals Frontfile Complete
subjects Amino acids
Bioconversions. Hemisynthesis
Biological and medical sciences
Bioreactors
Biotechnology
Chemical bonds
Ethanol
fluidized
Fluidized beds
Fundamental and applied biological sciences. Psychology
immobilized enzyme
L-aminoacylase
L-valine
Methods. Procedures. Technologies
packed bed reactors
Packed beds
Purification
Separation
Solubility
title Production of optically pure L-valine in fluidized and packed bed reactors with immobilized L-aminoacylase
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