Amidohydrolase Process: Expanding the use ofl-N-carbamoylase/N-succinyl-amino acid racemase tandem for theproduction of different optically pure l-amino acids
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Soriano Maldonado, Pablo![Autoridad Universidad de Almería Autoridad Universidad de Almería](/themes/Mirage2/images/autoridades/autoridad.png)
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Fecha
2014Resumen
tA bienzymatic system comprising an N-succinylamino acid racemase from Geobacillus kaustophilusCECT4264 (GkNSAAR) and an enantiospecific l-N-carbamoylase from Geobacillus stearothermophilusCECT43 (BsLcar) has been developed. This biocatalyst has been able to produce optically pure naturaland non-natural l-amino acids starting from racemic mixtures of N-acetyl-, N-formyl- and N-carbamoyl-amino acids by dynamic kinetic resolution. The fastest conversion rate was found with N-formyl-aminoacids, followed by N-carbamoyl- and N-acetyl-amino acids, and GkNSAAR proved to be the limiting stepof the system due to its lower specific activity. Metal ion cobalt was essential for the activity of thebiocatalyst and the system was optimally active when Co2+was added directly to the reaction mixture.The optimum pH for the biocatalyst proved to be 8.0, for both N-formyl- and N-carbamoyl-amino acidsubstrates, whereas optimum temperature ranges were 45–55◦C for N-formyl-amino acids and 55–70◦Cfor N-carbam...
Palabra/s clave
l-Amino acid
l-Amino acidN-Carbamoyl-l-amino acid amidohydrolase
l-Carbamoylase
l-CarbamoylaseN-Succinylamino acid racemase
Dynamic kinetic resolution
Biocatalysis
BiocatalysisCascade chemoenzymatic process
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