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@ARTICLE{Bollinger:888809,
      author       = {Bollinger, Alexander and Molitor, Rebecka and Thies,
                      Stephan and Koch, Rainhard and Coscolín, Cristina and
                      Ferrer, Manuel and Jaeger, Karl-Erich},
      title        = {{O}rganic-{S}olvent-{T}olerant {C}arboxylic {E}ster
                      {H}ydrolases for {O}rganic {S}ynthesis},
      journal      = {Applied and environmental microbiology},
      volume       = {86},
      number       = {9},
      issn         = {1098-5336},
      address      = {Washington, DC [u.a.]},
      publisher    = {Soc.},
      reportid     = {FZJ-2020-05223},
      pages        = {e00106-20},
      year         = {2020},
      abstract     = {Biocatalysis has emerged as an important tool in synthetic
                      organic chemistry enabling the chemical industry to execute
                      reactions with high regio- or enantioselectivity and under
                      usually mild reaction conditions while avoiding toxic waste.
                      Target substrates and products of reactions catalyzed by
                      carboxylic ester hydrolases are often poorly water soluble
                      and require organic solvents, whereas enzymes are evolved by
                      nature to be active in cells, i.e., in aqueous rather than
                      organic solvents. Therefore, biocatalysts that withstand
                      organic solvents are urgently needed. Current strategies to
                      identify such enzymes rely on laborious tests carried out by
                      incubation in different organic solvents and determination
                      of residual activity. Here, we describe a simple assay
                      useful for screening large libraries of carboxylic ester
                      hydrolases for resistance and activity in water-miscible
                      organic solvents. We have screened a set of 26 enzymes, most
                      of them identified in this study, with four different
                      water-miscible organic solvents. The triglyceride tributyrin
                      was used as a substrate, and fatty acids released by
                      enzymatic hydrolysis were detected by a pH shift indicated
                      by the indicator dye nitrazine yellow. With this strategy,
                      we succeeded in identifying a novel highly
                      organic-solvent-tolerant esterase from Pseudomonas
                      aestusnigri. In addition, the newly identified enzymes were
                      tested with sterically demanding substrates, which are
                      common in pharmaceutical intermediates, and two enzymes from
                      Alcanivorax borkumensis were identified which outcompeted
                      the gold standard ester hydrolase CalB from Candida
                      antarctica},
      cin          = {IMET},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IMET-20090612},
      pnm          = {581 - Biotechnology (POF3-581)},
      pid          = {G:(DE-HGF)POF3-581},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {32111588},
      UT           = {WOS:000529303800005},
      doi          = {10.1128/AEM.00106-20},
      url          = {https://juser.fz-juelich.de/record/888809},
}