Hydrolysis of PET and bis-(benzoyloxyethyl) terephthalate with a new polyesterase from Penicillium citrinum |
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Authors: | Stefan Liebminger Anita Eberl Fernanda Sousa Sonja Heumann Gudrun Fischer-Colbrie Artur Cavaco-Paulo Georg M Guebitz |
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Institution: |
a Research Centre of Applied Biocatalysis, Graz, Austria
b Graz University of Technology, Environmental Biotechnology, Graz, Austria
c Department of Textile Engineering, University of Minho, Guimaraes, Portugal |
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Abstract: | A polyethylene terephthalate (PET) model substrate, bis-(benzoyloxyethyl)terephthalate (3PET), was used to screen for micro-organisms producing enzymes hydrolyzing PET. From this screen, a strain growing on 3PET was isolated and identified as Penicillium citrinum. The polyesterase responsible for 3PET and PET hydrolysis was purified to electrophoretic homogeneity. The polyesterase had a molecular weight of 14.1 kDa, and the Km and Kcat values on 4-nitrophenyl butyrate were 0.57?mM and 0.21?s-1, respectively. Highest enzyme activities were obtained when P. citrinum was grown on a medium containing cutin, which was hydrolyzed by the polyesterase. Surface hydrolysis of PET with the enzyme lead to an increase in hydrophilicity based on rising height (+5.1?cm) and drop dissipation measurements (55?s). Both from PET and 3PET bis-(2-hydroxyethyl)terephthalate and mono-(2-hydroxyethyl)terephthalate were released, while only low amounts of terephthalic acid were liberated. |
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Keywords: | Polyethylene terephthalate polyesterase Penicillium citrinum |
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