Enzymatic transesterification of urethane-bond containing ester

Pia Skoczinski, Monica K. Espinoza Cangahuala, Dina Maniar, Katja Loos*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

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Abstract

Here we demonstrate the feasibility and successful application of enzymes in polyurethane network synthesis as well as occurring hurdles that have to be addressed when using urethanes synthesis substrates. The enzymatic transesterification of an urethane-bond containing monofunctional ester and a model alcohol carbitol using lipases is discussed. The reaction is optimized in terms of transesterification time and temperature, the reaction solvent, the possibility of a cosolvent and the alcohol amount, the used transesterification environment, and the biocatalyst. Enzymatic cross-linking of polyurethanes can open up a pool of new possibilities for cross-linking and related polyurethane network properties due to the enzymes high enantio-, stereo-, and regioselectivity and broad substrate spectrum. [Figure not available: see fulltext.]

Original languageEnglish
Number of pages13
JournalColloid and Polymer Science
DOIs
Publication statusPublished - 10-Jul-2020

Keywords

  • Polyurethanes
  • Transesterification
  • Biocatalysis
  • Lipase
  • Model study
  • THERMOMYCES-LANUGINOSUS LIPASE
  • CANDIDA-RUGOSA LIPASES
  • CATALYZED METHANOLYSIS
  • BIODIESEL PRODUCTION
  • FREE ROUTES
  • POLYURETHANES
  • ISOCYANATE
  • POLYMERIZATION
  • POLYAMIDES
  • VERSATILITY

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