RESUMO
Enantioselectivity has always been a key feature of enzymatic synthesis. In some cases, when enzymes are not strictly enantioselective, by tuning the reaction conditions it is possible to induce an enantioselective switch. A transaminase from Halomonas elongata (ω-HeWT), while generally S-selective, could be shifted towards generating the R-enantiomer at higher concentrations of amino acceptor or ionic strength, for example. Other enzymes are reported to have a similar behavior, and here we discuss some of them and their potential applications.
Assuntos
Transaminases , Biocatálise , EstereoisomerismoRESUMO
Enzymatic enantiopreference is one of the key advantages of biocatalysis. While exploring the synthesis of small cyclic (chiral amines) such as 3-aminotetrahydrofuran (THF-amine), using the (S)-selective transaminase from Halomonas elongata (HEwT), inversion of the enantiopreference was observed at increasing substrate loadings. In addition, the enantiopreference could be altered by variation of the ionic strength, or of the co-solvent content in the reaction mixture. For example, using otherwise identical reaction conditions, the presence of 2â M sodium chloride gave (R)-THF-amine (14 % ee), while the addition of 2.2â M isopropyl alcohol gave the (S)-enantiomer in 30 % ee. While the underlying cause is not currently understood, it appears likely that subtle changes in the structure of the enzyme cause the shift in enantiopreference and are worth exploring further.