Optimization of enzymatic ring-opening copolymerizations involving δ-gluconolactone as monomer by experimental design

Anamaria Todea, Emese Biro, Valentin Badea, Cristina Paul, Adinela Cimporescu, Lajos Nagy, Sándor Kéki, Geza Bandur, Carmen Boeriu, Francisc Péter

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Enzymatic incorporation of carbohydrate-derived monomer units into hydrophobic polyester backbones represents a promising alternative to obtain new biodegradable oligomers and polymers. Immobilized lipases are efficient biocatalysts for copolymerization of β-butyrolactone and δ-gluconolactone, but only a systematic optimization study was able to highlight the influence of the main reaction parameters on the polymerization degree and on the relative copolymer content of the product. Therefore, experimental design was employed for determination of the optimal ring-opening copolymerization conditions in solventless reaction systems, at temperatures up to 80°C. The obtained products, cyclic and linear polyesters, have been characterized by FT-IR, MALDI-TOF MS, NMR, and TG analysis, demonstrating the incorporation of gluconolactone unit(s) into the hydrophobic backbone of the polyester and the formation of new bio-based products.

Original languageEnglish
Pages (from-to)1781-1792
Number of pages12
JournalPure and Applied Chemistry
Volume86
Issue number11
DOIs
Publication statusPublished - Nov 1 2014

Keywords

  • Biocatalysis
  • Experimental design
  • Lipase
  • Modeling
  • POC-2014
  • Polymerization
  • δ-gluconolactone

ASJC Scopus subject areas

  • Chemistry(all)
  • Chemical Engineering(all)

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    Todea, A., Biro, E., Badea, V., Paul, C., Cimporescu, A., Nagy, L., Kéki, S., Bandur, G., Boeriu, C., & Péter, F. (2014). Optimization of enzymatic ring-opening copolymerizations involving δ-gluconolactone as monomer by experimental design. Pure and Applied Chemistry, 86(11), 1781-1792. https://doi.org/10.1515/pac-2014-0717