The PFE I shares some features with non-heme haloperoxidases and has been described
as a bifunctional enzyme – catalyzing both ester hydrolysis and halogenations [72].
The PFE I has been studied extensively over the past years [74-79]. Krebsfänger et al. [76]
purified it and determined parameters such as temperature and pH preferences, revealing a
broad pH profile with good activity between pH 5 and 10. The PFE I is active up to a
temperature of 70°C, however, it denatures rapidly at temperatures above 50°C.
Several substrates for the PFE I have been identified. In general, the preferred length of the
acyl chain is C2-C4, which is typical for an esterase [77]. While it is not very selective in the
resolution of chiral arylaliphatic acids like 3-phenylbutyrate, good enantioselectivity was
found in the resolution of a-phenyl ethanol. A moderate enantioselectivity was found in the
resolution of methyl-3-bromo-2-methyl propanoate (MBMP), while the selectivity against
methyl 2-chloropropionate (MCP) is rather low