Improving enzymatic polyurethane hydrolysis by tuning enzyme sorption

Caroline Gamerith, Enrique Herrero Acero, Alessandro Pellis, Andreas Ortner, Robert Vielnascher, Daniel Luschnig, Barbara Zartl, Karolina Haernvall, Sabine Zitzenbacher, Gernot Strohmeier, Oskar Hoff, Georg Steinkellner, Karl Gruber, Doris Ribitsch, Georg M. Guebitz

Research output: Contribution to journalArticlepeer-review


In this study we investigated the ability of amidases to hydrolyse polyurethane polyester co-polymers. In order to improve enzyme adsorption, a polyamidase from Nocardia farcinica (PA) was fused to a polymer binding module from a polyhydroxyalkanoate depolymerase from Alcaligenes faecalis (PA_PBM). The activity of these enzymes and of various commercially available amidases on a synthesized soluble model substrate was compared. The recombinant native PA showed the highest activity of 10.5 U/mg followed by PA_PBM with an activity of 1.13 U/mg. Both enzymes were able to cleave the urethane bond in polyurethane-polyesters with different degree of crystallinity as shown by FTIR. According to LC-TOF analysis the monomer 4,4′-diaminodiphenylmethane (MDA) and the oligomers 4-hydroxybutyl (3-(3-aminobenzyl)phenyl)carbamate, bis(4-hydroxybutyl) (methylenebis(3,1-phenylene))dicarbamate and 4-(((3-(3-(((4-hydroxybutoxy)carbonyl)amino)benzyl)phenyl)carbamoyl)oxy)butyl (4-hydroxybutyl) adipate were released. The polymer with a higher content of the rigid segment, MDA, was hydrolysed to a lower extent. Interestingly, despite the lower activity on the soluble model substrate, the PA_PBM fusion enzyme was up to 4 times more active on the polymer when compared with the native enzyme, confirming the relevance of enzyme adsorption for efficient hydrolysis.
Original languageEnglish
Pages (from-to)69-77
Number of pages9
JournalPolymer degradation and stability
Publication statusPublished - 4 Mar 2016


  • Polyurethane
  • Polyamidase
  • Enzymatic degradation
  • Polyurethane model substrate
  • Functionalization


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