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Cainelli, G. et al.

Cainelli, Engel, Galletti, Giacomini, Gualandi, Paradisi,

Engineered phenylalanine dehydrogenase in organic solvents: homogeneous and biphasic enzymatic reactions.

The use of engineered phenylalanine dehydrogenase N145A supported on Celite for the reductive amination of phenylpyruvic acid in homogeneous and biphasic aqueous-organic solvents is reported. The results indicate that the immobilised biocatalyst is remarkably robust, even in the presence of high concentrations of polar or non-polar organic solvents such as acetone, methanol, n-hexane, toluene and methylene chloride. Cofactor regeneration with alcohol dehydrogenase from Saccharomyces cerevisiae and ethanol was successfully explored. Application to the non-natural poorly water-soluble 2-oxo acid p-NO(2)-phenylpyruvic acid was successfully performed, resulting in the biocatalytic synthesis of p-NO(2)-phenylalanine. In all cases 100% stereoselectivity for the production of the amino acid was retained.[1]

References

Engineered phenylalanine dehydrogenase in organic solvents: homogeneous and biphasic enzymatic reactions. Cainelli, G., Engel, P.C., Galletti, P., Giacomini, D., Gualandi, A., Paradisi, F. Org. Biomol. Chem. (2005) [Pubmed]

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