Enzymatic synthesis of poly-L-lactide-co-glycolide in the ionic liquid 1-butyl-3-methylimidazolium hexafluorophosphate

Bioprocess Biosyst Eng. 2010 Nov;33(9):1095-101. doi: 10.1007/s00449-010-0435-5. Epub 2010 May 21.

Abstract

This article reports the lipase-catalyzed ring-opening copolymerization of L-lactide (LLA) and glycolide using the commercially available ionic liquid 1-butyl-3-methylimidazolium hexafluorophosphate as solvent media. Candida antarctica lipase B, immobilized in an acrylic support was used as biocatalyst. The reaction temperature had a direct influence on yields and molecular weights of the copolymers as well as LLA incorporation. The materials presented semi-crystalline structures assessed by DSC and powder XR diffraction analyses.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biotechnology / methods*
  • Candida / enzymology*
  • Catalysis
  • Fungal Proteins
  • Imidazoles / chemistry*
  • Industrial Microbiology / methods
  • Ions
  • Lipase / chemistry*
  • Magnetic Resonance Spectroscopy / methods
  • Models, Chemical
  • Polyglactin 910 / chemistry*
  • Polymers / chemistry
  • Powders / chemistry
  • Temperature
  • Time Factors
  • X-Ray Diffraction

Substances

  • 1-butyl-3-methylimidazolium hexafluorophosphate
  • Fungal Proteins
  • Imidazoles
  • Ions
  • Polymers
  • Powders
  • Polyglactin 910
  • Lipase
  • lipase B, Candida antarctica