@article{BauchBoettcherBornscheueretal.2016,
  author    = {Bauch, Marcel and B{\"o}ttcher, Dominique and Bornscheuer, Uwe T. and Linker, Torsten},
  title     = {Enzymatic Cleavage of Aryl Acetates},
  series = {ChemCatChem : heterogeneous \& homogeneous \& bio- \& nano-catalysis ; a journal of ChemPubSoc Europe},
  volume    = {8},
  journal   = {ChemCatChem : heterogeneous \& homogeneous \& bio- \& nano-catalysis ; a journal of ChemPubSoc Europe},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  organization    = {HESS Collaboration},
  issn      = {1867-3880},
  doi       = {10.1002/cctc.201600678},
  pages     = {2853 -- 2857},
  year      = {2016},
  abstract  = {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.},
  language  = {en}
}