@article{ReinickeReesEspeeletal.2017,
  author    = {Reinicke, Stefan and Rees, Huw C. and Espeel, Pieter and Vanparijs, Nane and Bisterfeld, Carolin and Dick, Markus and Rosencrantz, Ruben R. and Brezesinski, Gerald and de Geest, Bruno G. and Du Prez, Filip E. and Pietruszka, J{\"o}rg and B{\"o}ker, Alexander},
  title     = {Immobilization of 2-Deoxy-D-ribose-5-phosphate Aldolase in Polymeric Thin Films via the Langmuir-Schaefer Technique},
  series = {ACS applied materials \& interfaces},
  volume    = {9},
  journal   = {ACS applied materials \& interfaces},
  publisher = {American Chemical Society},
  address   = {Washington},
  issn      = {1944-8244},
  doi       = {10.1021/acsami.6b13632},
  pages     = {8317 -- 8326},
  year      = {2017},
  abstract  = {A synthetic protocol for the fabrication of ultrathin polymeric films containing the enzyme 2-deoxy-D-ribose-5-phosphate aldolase from Escherichia coli (DERA(EC)) is presented. Ultrathin enzymatically active films are useful for applications in which only small quantities of active material are needed and at the same time quick response and contact times without diffusion limitation are wanted. We show how DERA as an exemplary enzyme can be immobilized in a thin polymer layer at the air-water interface and transferred to a suitable support by the Langmuir-Schaefer technique under full conservation of enzymatic activity. The polymer in use is a poly(N-isopropylacrylamide-co-N-2-thiolactone acrylamide) (P(NIPAAm-co-TlaAm)) statistical copolymer in which the thiolactone units serve a multitude of purposes including hydrophobization of the polymer, covalent binding of the enzyme and the support and finally cross-linking of the polymer matrix. The application of this type of polymer keeps the whole approach simple as additional cocomponents such as cross-linkers are avoided.},
  language  = {en}
}
@article{ZhangBisterfeldBramskietal.2017,
  author    = {Zhang, Shuhao and Bisterfeld, Carolin and Bramski, Julia and Vanparijs, Nane and De Geest, Bruno G. and Pietruszka, J{\"o}rg and B{\"o}ker, Alexander and Reinicke, Stefan},
  title     = {Biocatalytically Active Thin Films via Self-Assembly of 2-Deoxy-D-ribose-5-phosphate Aldolase-Poly(N-isopropylacrylamide) Conjugates},
  series = {Bioconjugate chemistry},
  volume    = {29},
  journal   = {Bioconjugate chemistry},
  number    = {1},
  publisher = {American Chemical Society},
  address   = {Washington},
  issn      = {1043-1802},
  doi       = {10.1021/acs.bioconjchem.7b00645},
  pages     = {104 -- 116},
  year      = {2017},
  abstract  = {2-Deoxy-D-ribose-5-phosphate aldolase (DERA) is a biocatalyst that is capable of converting acetaldehyde and a second aldehyde as acceptor into enantiomerically pure mono- and diyhydroxyaldehydes, which are important structural motifs in a number of pharmaceutically active compounds. However, substrate as well as product inhibition requires a more-sophisticated process design for the synthesis of these motifs. One way to do so is to the couple aldehyde conversion with transport processes, which, in turn, would require an immobilization of the enzyme within a thin film that can be deposited on a membrane support. Consequently, we developed a fabrication process for such films that is based on the formation of DERA-poly(N-isopropylacrylamide) conjugates that are subsequently allowed to self-assemble at an air-water interface to yield the respective film. In this contribution, we discuss the conjugation conditions, investigate the interfacial properties of the conjugates, and, finally, demonstrate a successful film formation under the preservation of enzymatic activity.},
  language  = {en}
}