Enzymes for the Biofunctionalization of Poly(Ethylene Terephthalate)

  • Wolfgang ZimmermannEmail author
  • Susan Billig
Part of the Advances in Biochemical Engineering / Biotechnology book series (ABE, volume 125)


The functionalization of synthetic polymers such as poly(ethylene terephthalate) to improve their hydrophilicity can be achieved biocatalytically using hydrolytic enzymes. A number of cutinases, lipases, and esterases active on polyethylene terephthalate have been identified and characterized. Enzymes from Fusarium solani, Thermomyces insolens, T. lanuginosus, Aspergillus oryzae, Pseudomonas mendocina, and Thermobifida fusca have been studied in detail. Thermostable biocatalysts hydrolyzing poly(ethylene terephthalate) are promising candidates for the further optimization of suitable biofunctionalization processes for textile finishing, technical, and biomedical applications.

Graphical Abstract


Biofunctionalization Cutinase Enzymes Esterase Lipase Poly(ethylene terephthalate) Polyester Thermostability 



Atomic force microscopy


Ethylene glycol dibenzyl ester


bis(2-hydroxyethyl terephthalate)


bis(3-hydroxypropyl terephthalate)


Cyclo-tris–ethylene terephthalate, cyclic PET trimer


Diethyl terephthalate


Dimethyl terephthalate


Diethyl p-phthalate


Differential scanning calorimetry




1,2-Ethylene-mono-terephthalate-mono(2-hydroxyethyl terephthalate)


Electron spectroscopy for chemical analysis


Fourier transform infrared spectroscopy


High performance liquid chromatography


Monoethylene glycol


mono(2-hydroxyethyl) terephthalate


mono(3-hydroxypropyl) terephthalate




Polyethylene glycol


Poly(ethylene terephthalate)

PET dimer

bis-(p-methylbenzoic acid)-ethylene glycol ester

PET trimer

bis(benzoyloxyethyl) terephthalate


Poly(trimethylene terephthalate)




Scanning electron microscopy

Triton X-100

Octyl phenoxy polyethoxy ethanol


Glass transition temperature


Thermal denaturation temperature


Melting temperature


Thin layer chromatography


Terephthalic acid


X-ray photoelectron spectroscopy


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© Springer-Verlag Berlin Heidelberg 2010

Authors and Affiliations

  1. 1.Department of Microbiology and Bioprocess Technology, Institute of BiochemistryUniversity of LeipzigLeipzigGermany

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