Enzymatic modification of poly(ethylene terephtalate

M.A.M.E. Vertommen, Vincent Nierstrasz, M. van der Veer, M. van der Veer, Marinus Warmoeskerken

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Abstract

This study unambiguously confirms hydrolysis using cutinase of the persistent synthetic polymer poly(ethylene terephthalate), the most important synthetic fiber in the textile industry by direct measurement and identification of the different hydrolysis products. In this aqueous heterogeneous system, dissolved cutinase from Fusarium solani pisi acts on different solid poly(ethylene terephthalate) substrates. The extent of hydrolysis was detected by measuring the amount of (soluble) degradation products in solution using reversed-phase HPLC. Crystallinity greatly affects the capability of the enzyme to hydrolyze the ester bonds, displaying relatively high activity towards an amorphous polyester film and little activity on a highly crystalline substrate. The enzyme is sufficiently stable, hydrolysis rate on the amorphous substrate maintained at sufficient high level over a long period of time of at least five days. From an industrial point of view it is highly recommended to increase the hydrolysis rates.
Original languageUndefined
Pages (from-to)376-386
Number of pages11
JournalJournal of biotechnology
Volume120
Issue number4
DOIs
Publication statusPublished - 2005

Keywords

  • Heterogeneous catalysis
  • Cutinase
  • Polyester
  • HPLC
  • IR-77638
  • METIS-229672
  • Lipase

Cite this

Vertommen, M. A. M. E., Nierstrasz, V., van der Veer, M., van der Veer, M., & Warmoeskerken, M. (2005). Enzymatic modification of poly(ethylene terephtalate. Journal of biotechnology, 120(4), 376-386. https://doi.org/10.1016/j.jbiotec.2005.06.015