@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}
}
@article{ReinickeFischerBramskietal.2019,
  author    = {Reinicke, Stefan and Fischer, Thilo and Bramski, Julia and Pietruszka, J{\"o}rg and B{\"o}ker, Alexander},
  title     = {Biocatalytically active microgels by precipitation polymerization of N-isopropyl acrylamide in the presence of an enzyme},
  series = {RSC Advances},
  volume    = {9},
  journal   = {RSC Advances},
  number    = {49},
  publisher = {Royal Society of Chemistry},
  address   = {Cambridge},
  issn      = {2046-2069},
  doi       = {10.1039/c9ra04000e},
  pages     = {28377 -- 28386},
  year      = {2019},
  abstract  = {We present a novel protocol for the synthesis of enzymatically active microgels. The protocol is based on the precipitation polymerization of N-isopropylacrylamide (NIPAm) in the presence of an enzyme and a protein binding comonomer. A basic investigation on the influence of different reaction parameters such as monomer concentration and reaction temperature on the microgel size and size distribution is performed and immobilization yields are determined. Microgels exhibiting hydrodynamic diameters between 100 nm and 1 mu m and narrow size distribution could be synthesized while about 31-44\% of the enzyme present in the initial reaction mixture can be immobilized. Successful immobilization including a verification of enzymatic activity of the microgels is achieved for glucose oxidase (GOx) and 2-deoxy-d-ribose-5-phosphate aldolase (DERA). The thermoresponsive properties of the microgels are assessed and discussed in the light of activity evolution with temperature. The positive correlation of enzymatic activity with temperature for the GOx containing microgel originates from a direct interaction of the enzyme with the PNIPAm based polymer matrix whose magnitude is highly influenced by temperature.},
  language  = {en}
}