Enzymatic surface modification of poly(ethylene terephthalate).
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.
Vertommen
M A M E
MA
Textile Technology Group, Department of Science and Technology, University of Twente, P.O. Box 217, 7500 AE Enschede, The Netherlands.
Nierstrasz
V A
VA
Veer
M van der
Mv
Warmoeskerken
M M C G
MM
D002265:Carboxylic Ester Hydrolases / Q000737:chemistry*; D004800:Enzymes, Immobilized / Q000737:chemistry; D005656:Fungal Proteins / Q000737:chemistry*; D005670:Fusarium / Q000201:enzymology*; D006868:Hydrolysis; D011093:Polyethylene Terephthalates / Q000737:chemistry*
D004800:Enzymes, Immobilized; D005656:Fungal Proteins; D011093:Polyethylene Terephthalates; D002265:Carboxylic Ester Hydrolases; C019952:cutinase