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

✍ Scribed by A Bódalo-Santoyo; J L Gómez-Carrasco; E Gómez-Gómez; J Bastida-Rodriquez; M F Máximo-Martín; A M Hidalgo-Montesinos

• Publisher: Wiley (John Wiley & Sons)
• Year: 1999
• Tongue: English
• Weight: 92 KB
• Volume: 74
• Category: Article
• ISSN: 0268-2575
• DOI: 10.1002/(sici)1097-4660(199905)74:5<403::aid-jctb51>3.0.co;2-n

✦ Synopsis

A process to obtain L-valine has been developed using ¯uidized 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 ¯uidized and packed bed reactors was studied at three different substrate concentrations and two different ¯ow 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 ef¯uents. The amount of added ethanol did not in¯uence 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.