Enzymatic modification of poly(ethylene terephtalate

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

Research output: Contribution to journalArticleAcademicpeer-review

164 Citations (Scopus)

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
Vertommen, M.A.M.E. ; Nierstrasz, Vincent ; van der Veer, M. ; van der Veer, M. ; Warmoeskerken, Marinus. / Enzymatic modification of poly(ethylene terephtalate. In: Journal of biotechnology. 2005 ; Vol. 120, No. 4. pp. 376-386.
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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.",
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Vertommen, MAME, Nierstrasz, V, van der Veer, M, van der Veer, M & Warmoeskerken, M 2005, 'Enzymatic modification of poly(ethylene terephtalate', Journal of biotechnology, vol. 120, no. 4, pp. 376-386. https://doi.org/10.1016/j.jbiotec.2005.06.015

Enzymatic modification of poly(ethylene terephtalate. / Vertommen, M.A.M.E.; Nierstrasz, Vincent; van der Veer, M.; van der Veer, M.; Warmoeskerken, Marinus.

In: Journal of biotechnology, Vol. 120, No. 4, 2005, p. 376-386.

Research output: Contribution to journalArticleAcademicpeer-review

TY - JOUR

T1 - Enzymatic modification of poly(ethylene terephtalate

AU - Vertommen, M.A.M.E.

AU - Nierstrasz, Vincent

AU - van der Veer, M.

AU - van der Veer, M.

AU - Warmoeskerken, Marinus

PY - 2005

Y1 - 2005

N2 - 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.

AB - 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.

KW - Heterogeneous catalysis

KW - Cutinase

KW - Polyester

KW - HPLC

KW - IR-77638

KW - METIS-229672

KW - Lipase

U2 - 10.1016/j.jbiotec.2005.06.015

DO - 10.1016/j.jbiotec.2005.06.015

M3 - Article

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JO - Journal of biotechnology

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