Rational re-design of the “double-racemase hydantoinase process” for optically pure production of natural and non-natural l-amino acids
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Rodriguez-Alonso, M.J.; Clemente Jiménez, Josefa María; Rodríguez Vico, Felipe; Las Heras Vázquez, Francisco JavierFecha
2015Resumen
The “hydantoinase process” is a well-established method for the industrial production of optically pure
d-amino acids. However, due to the strict d-enantioselectivity of most hydantoinase enzymes, the process
is less efficient for l-amino acid production. We present a new chemo-enzymatic cascade reaction for
natural and non-natural l-amino acid production from racemic mixtures of 5-monosubstituted hydantoins.
This system comprised the following enzymes: d-hydantoinase from Agrobacterium tumefaciens
BQL9, hydantoin racemase 1 from A. tumefaciens C58 and l-N-carbamoylase from Geobacillus stearothermophilus
CECT43, together with N-succinyl-amino acid racemase from G. kaustophilus CECT4264. This
latter presents catalytic promiscuity and racemizes N-carbamoyl-amino acids. This activity avoids the
accumulation of N-carbamoyl-d-amino acid in the reaction due to the strict d-enantioselectivity of the
hydantoinase. The optimum pH for the system proved to be 8.0, whereas optimum tempera...
Palabra/s clave
Hydantoinase process
d-Hydantoinase
l-N-Carbamoylase
Hydantoin racemase
N-Succinyl-amino acid racemase
Double-racemase
Enzymatic cascade reaction
l-Amino acids