Journal
CHEMCATCHEM
Volume 11, Issue 10, Pages 2490-2499Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cctc.201900451
Keywords
PEGylation; esterases; activity; catalysis; polyester
Categories
Funding
- Portuguese Foundation for Science and Technology (FCT) - European Regional Development Fund [UID/BIO/04469/2019, NORTE-01-0145-FEDER-000004]
- FCT [SFRH/BD/121673/2016, SFRH/BD/114684/2016, SFRH/BPD/98388/2013, SFRH/IF/00186/2015]
- European Union through the European Regional Development Fund (ERDF) under the Competitiveness Operational Program [POC-A1.1.4-E-2015, 30/01.09.2016]
- Project Search-ON2: Revitalization of HPC infrastructure of UMinho [NORTE-07-0162-FEDER-000086]
- Fundação para a Ciência e a Tecnologia [SFRH/BD/114684/2016] Funding Source: FCT
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In this work we explored PEGylation as an efficient strategy to improve esterase's catalytic performance. For this, we PEGylated three esterases, namely lipase from Candida antarctica B (CALB), lipase from Thermomyces lanuginosus (TL) and cutinase from Fusarium solani pisi (CUT) and evaluated their catalytic performance by using the biosynthesis of poly(ethylene glutarate) as model reaction. After PEGylation with a 5 kDa aldehyde-PEG, CALB and cutinase revealed an increase of activity against pnitrophenyl butyrate hydrolysis (2-fold of increase for CALB and 4-fold of increase for cutinase). Unmodified and PEGylated lipase TL displayed however similar activity results. The polymerase activity of native and PEGylated esterases was also assessed. The data revealed a higher polymerase activity for the lipase TL and cutinase PEGylated forms (88% conversion for PEG-lipase TL and 34% for PEG-cutinase). Molecular dynamics were used to evaluate the effect of PEG on the geometry of the active site of enzymes with lid domain (TL and CALB). These studies corroborate the experimental data revealing a more open active site cavity for the PEGylated catalysts facilitating the catalysis.
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