TY  - JOUR
A1  - Bauch, Marcel
A1  - Böttcher, Dominique
A1  - Bornscheuer, Uwe T.
A1  - Linker, Torsten
T1  - Enzymatic Cleavage of Aryl Acetates
JF  - ChemCatChem : heterogeneous & homogeneous & bio- & nano-catalysis ; a journal of ChemPubSoc Europe
N2  - Seven enzymes have been screened for the cleavage of aryl acetates. Phenyl and naphthyl acetates react with lipases and esterases, whereas the sterically demanding anthracene acetate gave a conversion only with porcine liver esterase and esterase 2 from Bacillus subtilis (BS2). These two enzymes have been employed on a preparative (0.5 mmol) scale and afforded cleavage products in 91 and 94% yields, even for anthracene acetate. Thus, this method is superior to chemical cleavage with catalytic amounts of sodium methoxide (Zemplen conditions), which gave only low conversions. Finally, regioselectivity has been achieved with an anthracene bisacetate, in which an ethyl group controls the cleavage of the first acetate. This indicates that steric interactions play a crucial role in the enzymatic cleavage of aryl acetates, which might be interesting for future applications or the development of enzyme inhibitors.
KW  - arenes
KW  - enzyme catalysis
KW  - regioselectivity
KW  - steric hindrance
KW  - substituent effects
Y1  - 2016
U6  - https://doi.org/10.1002/cctc.201600678
SN  - 1867-3880
SN  - 1867-3899
VL  - 8
SP  - 2853
EP  - 2857
PB  - Wiley-VCH
CY  - Weinheim
ER  -