@article{SchoeneKratzSchulzetal.2016,
  author    = {Sch{\"o}ne, Anne-Christin and Kratz, Karl and Schulz, Burkhard and Lendlein, Andreas},
  title     = {Polymer architecture versus chemical structure as adjusting tools for the enzymatic degradation of oligo(epsilon-caprolactone) based films at the air-water interface},
  series = {Polymer Degradation and Stability},
  volume    = {131},
  journal   = {Polymer Degradation and Stability},
  publisher = {Elsevier},
  address   = {Oxford},
  issn      = {0141-3910},
  doi       = {10.1016/j.polymdegradstab.2016.07.010},
  pages     = {114 -- 121},
  year      = {2016},
  abstract  = {The enzymatic degradation of oligo(epsilon-caprolactone) (OCL) based films at the air-water interface is investigated by Langmuir monolayer degradation (LMD) experiments to elucidate the influence of the molecular architecture and of the chemical structure on the chain scission process. For that purpose, the interactions of 2D monolayers of two star-shaped poly(epsilon-caprolactone)s (PCLs) and three linear OCL based copolyesterurethanes (P(OCL-U)) with the lipase from Pseudomonas cepacia are evaluated in comparison to linear OCL. While the architecture of star-shaped PCL Langmuir layers slightly influences their degradability compared to OCL films, significantly retarded degradations are observed for P(OCL-U) films containing urethane junction units derived from 2, 2 (4), 4-trimethyl hexamethylene diisocyanate (TMDI), hexamethylene diisocyanate (HDI) or lysine ethyl ester diisocyanate (LDI). The enzymatic degradation of the OCL based 2D structures is related to the presence of hydrophilic groups within the macromolecules rather than to the packing density of the film or to the molecular weight. The results reveal that the LMD technique allows the parallel analysis of both the film/enzyme interactions and the degradation process on the molecular level. (C) 2016 Elsevier Ltd. All rights reserved.},
  language  = {en}
}
@article{SchoeneKratzSchulzetal.2016,
  author    = {Sch{\"o}ne, Anne-Christin and Kratz, Karl and Schulz, Burkhard and Lendlein, Andreas},
  title     = {The relevance of hydrophobic segments in multiblock copolyesterurethanes for their enzymatic degradation at the air-water interface},
  series = {Polymer : the international journal for the science and technology of polymers},
  volume    = {102},
  journal   = {Polymer : the international journal for the science and technology of polymers},
  publisher = {Elsevier},
  address   = {Oxford},
  issn      = {0032-3861},
  doi       = {10.1016/j.polymer.2016.09.001},
  pages     = {92 -- 98},
  year      = {2016},
  abstract  = {The interplay of an enzyme with a multiblock copolymer PDLCL containing two segments of different hydrophilicity and degradability is explored in thin films at the air-water interface. The enzymatic degradation was studied in homogenous Langmuir monolayers, which are formed when containing more than 40 wt\% oligo(epsilon-caprolactone) (OCL). Enzymatic degradation rates were significantly reduced with increasing content of hydrophobic oligo(omega-pentadecalactone) (OPDL). The apparent deceleration of the enzymatic process is caused by smaller portion of water-soluble degradation fragments formed from degradable OCL fragments. Beside the film degradation, a second competing process occurs after adding lipase from Pseudomonas cepacia into the subphase, namely the enrichment of the lipase molecules in the polymeric monolayer. The incorporation of the lipase into the Langmuir film is experimentally revealed by concurrent surface area enlargement and by Brewster angle microscopy (BAM). Aside from the ability to provide information about the degradation behavior of polymers, the Langmuir monolayer degradation (LMD) approach enables to investigate polymer-enzyme interactions for non-degradable polymers. (C) 2016 Elsevier Ltd. All rights reserved.},
  language  = {en}
}