10.3987/COM-10-S(E)60
The research focused on the synthesis and characterization of 2-amino-3-(5-phenylfuran-2-yl)propionic acids and 5-phenylfuran-2-ylacrylic acids, which were found to be novel substrates for phenylalanine ammonia-lyase (PAL). The purpose of the study was to explore the enzyme's ability to catalyze the conversion of these compounds and to isolate their D- and L-enantiomers. The researchers synthesized the compounds and characterized them using various spectroscopic techniques. They then used recombinant PAL to convert the racemic mixtures into their corresponding acrylates, from which the D-enantiomers were isolated. Conversely, L-enantiomers were prepared by reversing the PAL reaction in the presence of 6 M ammonia at pH 10. The study concluded that these new compounds are good substrates for recombinant PAL and can be resolved into their enantiomers through biocatalysis. The chemicals used in the process included various anilines, furan-2-carbaldehyde, triphenyl-λ5-phosphanilidene acetic acid ethyl ester, and other reagents and solvents for the synthesis and characterization of the novel furanylalanines.