“In-situ” lipase-catalyzed cotton coating with polyesters from ethylene glycol and glycerol

Xin, Zhao; Noro, Jennifer; Fu, Jiajia; Wang, Hongbo; Silva, Carla; Cavaco-Paulo, Artur

doi:10.1016/j.procbio.2018.01.002

Cited by 15 publications

(10 citation statements)

References 33 publications

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“…Many reports using CALB as catalyst for the polyester synthesis are found in literature, however the use of native lipase TL for this purpose is still poorly explored. Zhao et al ., reported the in situ coating of cotton with polyesters synthesised by lipase TL and CALB. In their work the polyester synthesis was carried out using different amounts of each enzyme, and for this reason it was hard to distinguish their catalytic behaviour for the same substrate.…”

Section: Resultsmentioning

confidence: 99%

Catalytic Activation of Esterases by PEGylation for Polyester Synthesis

et al. 2019

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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 p‐nitrophenyl 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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Section: Resultsmentioning

confidence: 99%

Catalytic Activation of Esterases by PEGylation for Polyester Synthesis

et al. 2019

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“…Pentaethylene glycol and hexaethylene glycol, present in sample CM3, are members of the homologous series of polyethylene glycols commonly used as raw materials in a large number of industrial applications such as the condensation with dimethyl terephthalate or terephthalic acid resulting in a polyester resin [56]. Dimethyl succinate, identified in the same sample, is a starting reactant used in the synthesis of some polyesters [57].…”

Section: Hs-spme-gc-msmentioning

confidence: 99%

Characterization of Polyester Coatings Intended for Food Contact by Different Analytical Techniques and Migration Testing by LC-MSn

et al. 2022

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Polymeric coating formulations may contain different components such as cross-linking agents, resins, lubricants, and solvents, among others. If the reaction process or curing conditions are not applied in a proper way, these components may remain unreacted in the polymeric network and could be released and migrate into foods. In this study, several polyester coatings intended for food contact were investigated. Firstly, Fourier-transform infrared spectroscopy with an attenuated total reflectance (ATR-FTIR) spectrometer and confocal Raman microscopy were used to identify the type of coating. Then, different techniques, including gas chromatography coupled to mass spectrometry (GC-MS) and analysis by matrix-assisted laser desorption coupled to time-of-flight mass spectrometry (MALDI-TOF-MS), among others, were used to investigate the potential volatile and non-volatile migrants. Moreover, migration assays were carried out to evaluate the presence of monomers and to tentatively identify possible oligomers below 1000 Da. The analyses were performed by liquid chromatography coupled to ion trap mass spectrometry (LC-MSn). Using the information collected from each analytical technique, it was possible to elucidate some of the starting substances used in the formulation of the polyester coatings analyzed in this study. In migration tests, several polyester oligomers were tentatively identified for which there is not toxicological data available and, therefore, no migration limits established to date.

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“…Many reports using CALB as catalyst for the polyester synthesis are found in literature, however the use of native lipase TL for this purpose is still poorly explored. Zhao et al, [17] reported the in situ coating of cotton with polyesters synthesised by lipase TL and CALB. In their work the polyester synthesis was carried out using different amounts of each enzyme, and for this reason it was hard to distinguish their catalytic behaviour for the same substrate.…”

Section: Effect Of Pegylation On the Polymerase Activity Of Esterasesmentioning

confidence: 99%

Catalytic activation of esterases by PEGylation for polyester synthesis

Silva¹,

Noro²,

Castro³

et al. 2020

Preprint

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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.

show abstract

“In-situ” lipase-catalyzed cotton coating with polyesters from ethylene glycol and glycerol

Cited by 15 publications

References 33 publications

Catalytic Activation of Esterases by PEGylation for Polyester Synthesis

Catalytic Activation of Esterases by PEGylation for Polyester Synthesis

Characterization of Polyester Coatings Intended for Food Contact by Different Analytical Techniques and Migration Testing by LC-MSn

Catalytic activation of esterases by PEGylation for polyester synthesis

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