Hydrolysis of PET and bis-(benzoyloxyethyl) terephthalate with a new polyesterase from<i>Penicillium citrinum</i>

Liebminger, Stefan; Eberl, Anita; Sousa, Fernanda Severo Sabedra; Heumann, Sonja; Fischer-Colbrie, Gudrun; Cavaco‐Paulo, Artur; Guebitz, Georg M.

doi:10.1080/10242420701379734

Cited by 116 publications

(76 citation statements)

References 23 publications

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“…In contrast, this behaviour was not observed for the lipase where the ratio of BA to HEB always remained constant (up to one week of incubation) indicating that HEB cannot be hydrolysed by this enzyme. Similar properties were previously found for a polyesterase from Penicillium citrinum (Liebminger et al, 2007).…”

Section: Resultssupporting

confidence: 82%

Enzymatic surface hydrolysis of poly(ethylene terephthalate) and bis(benzoyloxyethyl) terephthalate by lipase and cutinase in the presence of surface active molecules

Eberl

Heumann

Brückner

et al. 2009

Journal of Biotechnology

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A lipase from Thermomyces lanuginosus and cutinases from Thermobifida fusca and Fusarium solani hydrolysed poly(ethylene terephthalate) (PET) fabrics and films and bis(benzoyloxyethyl) terephthalate (3PET) endo-wise as shown by MALDI-Tof-MS, LC-UVD/MS, cationic dyeing and XPS analysis. Due to interfacial activation of the lipase in the presence of Triton X-100, a seven-fold increase of hydrolysis products released from 3PET was measured. In the presence of the plasticizer N,N-diethyl-2-phenylacetamide (DEPA), increased hydrolysis rates of semi-crystalline PET films and fabrics were measured both for lipase and cutinase. The formation of novel polar groups resulted in enhanced dye ability with additional increase in colour depth by 130% and 300% for cutinase and lipase, respectively, in the presence of plasticizer.

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Section: Resultssupporting

confidence: 82%

Enzymatic surface hydrolysis of poly(ethylene terephthalate) and bis(benzoyloxyethyl) terephthalate by lipase and cutinase in the presence of surface active molecules

Eberl

Heumann

Brückner

et al. 2009

Journal of Biotechnology

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212

170

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“…Among cutinases, representatives from Aspergilllus oryzae, Humicola insolens [35], Penicillium citrinum [36], Fusarium solani [30,37], Thermobifida fusca [29] and Thermobifida cellulolysitica [27] have been described to hydrolyze PET. Considerably fewer lipases have been described to hydrolyze PET, including enzymes from Candida antarctica [25], Thermomyces lanuginosus [32], Burkholderia spp.…”

Section: Introductionmentioning

confidence: 99%

A New Esterase from Thermobifida halotolerans Hydrolyses Polyethylene Terephthalate (PET) and Polylactic Acid (PLA)

et al. 2012

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Abstract:A new esterase from Thermobifida halotolerans (Thh_Est) was cloned and expressed in E. coli and investigated for surface hydrolysis of polylactic acid (PLA) and polyethylene terephthalate (PET). Thh_Est is a member of the serine hydrolases superfamily containing the -GxSxG-motif with 85-87% homology to an esterase from T. alba, to an acetylxylan esterase from T. fusca and to various Thermobifida cutinases. Thh_Est hydrolyzed the PET model substrate bis(benzoyloxyethyl)terephthalate and PET releasing terephthalic acid and mono-(2-hydroxyethyl) terephthalate in comparable amounts (19.8 and 21.5 mmol/mol of enzyme) while no higher oligomers like bis-(2-hydroxyethyl) terephthalate were detected. Similarly, PLA was hydrolyzed as indicated by the release of lactic acid. Enzymatic surface hydrolysis of PET and PLA led to a strong hydrophilicity increase, as quantified with a WCA decrease from 90.8° and 75.5° to 50.4° and to a complete spread of the water drop on the surface, respectively. OPEN ACCESSPolymers 2012, 4 618

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“…[7,13,20] Thus, it was interesting to know, whether PET-hydrolases from other enzyme classes such as the lipase from T. lanuginosus [3] would also show cutinase activity. Consequently, a GC-MS based technique was successfully established and products released by the enzymes from cutin were analysed.…”

Section: Resultsmentioning

confidence: 99%

Hydrolysis of Cutin by PET‐Hydrolases

Korpecka

Heumann

Billig

et al. 2010

Macromolecular Symposia

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Summary: Functionalisation of synthetic polymers by using enzymes has been recently demonstrated. The major advantage of enzymes over chemical processes lies in their surface specific and endo-wise mode of action. Surface hydrophilisation of PET with lipases and cutinases leads to a dramatic increase of the surfacial acid and hydroxyl group content while conventional chemical treatment does not cause any change. However, this PET-hydrolysing activity by enzymes from distinct classes has not yet been correlated to activity on natural polyesters. Here, we show that lipases, cutinases and a PHA-depolymerase are all capable of hydrolysing PET, while only lipases and cutinases also hydrolysed cutin to various degrees. Lipases showed a higher specificity for terminal fatty acids while the cutinases preferred hydroxy fatty acids during cutin hydrolysis.

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Hydrolysis of PET and bis-(benzoyloxyethyl) terephthalate with a new polyesterase fromPenicillium citrinum

Cited by 116 publications

References 23 publications

Enzymatic surface hydrolysis of poly(ethylene terephthalate) and bis(benzoyloxyethyl) terephthalate by lipase and cutinase in the presence of surface active molecules

Enzymatic surface hydrolysis of poly(ethylene terephthalate) and bis(benzoyloxyethyl) terephthalate by lipase and cutinase in the presence of surface active molecules

A New Esterase from Thermobifida halotolerans Hydrolyses Polyethylene Terephthalate (PET) and Polylactic Acid (PLA)

Hydrolysis of Cutin by PET‐Hydrolases

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