The effect of high-energy environments on the structure of laccase-polymerized poly(catechol)

Su, Jing; Castro, Tarsila G.; Noro, Jennifer; Fu, Jiajia; Wang, Qiang; Silva, Carla; Cavaco-Paulo, Artur

doi:10.1016/j.ultsonch.2018.05.033

Cited by 23 publications

(36 citation statements)

References 37 publications

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“…Despite the lower coating, PET fibres are also colourized independently on the catalyst used. This corroborates our previous findings [23] where we studied for the first time the in situ enzymatic colouration of PET using native laccase. Herein, we confirm these results and deepen the study by using chemically modified laccases which incremented the polymerization.…”

Section: "In Situ" Colouration Of Fabricssupporting

confidence: 92%

“…In previous studies, we explored the role of high energy environments on the enzymatic polymerization of catechol. Our findings suggested that the use of devices like high-pressure homogenizers (HPH) for the enzymatic polymerization of phenolics greatly improve the conversion rates and polymerization degrees [23]. High-pressure homogenization is a technology generally applied to reduce the particles size using continuous or semi-continuous pressures between 60-400 M P [24].…”

Section: Introductionmentioning

confidence: 92%

“…These findings have been reported previously by us (data not shown) where we found that the chemically modified laccases are able to improve the polymerization of catechol. Moreover, the role of highenergy environments was also previously described as potentiating the enzymatic polymerization to produce higher polymers and convert higher amount of monomer [23,26]. A higher amount of produced oligomers and polymers not always corresponds to a higher deposition onto the fibre substrates used as containers.…”

Section: Catechol and P-phenylenediamine Polymerizationmentioning

confidence: 99%

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Coloured and low conductive fabrics by in situ laccase-catalysed polymerization

Noro

et al. 2019

Process Biochemistry

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Coloured and conductive fabrics were obtained through "in situ" laccase polymerization of catechol and pphenylenediamine under high-pressure homogenization. Both monomers, catechol and p-phenylenediamine, were polymerized by different laccase forms, namely native, PEGylated and Epoxy-PEGylated. All the catalysts were placed inside a textile fabric bag which served simultaneously as enzyme support and as substrate for coating with the newly produced polymers. The PEGylated laccase forms gave rise to a higher amount of oligomers/polymers and higher colouration level of polyethylene terephthalate (PET), cotton and wool fabrics compared to native laccase. Both functional polymers were able to confer conductivity to the substrates however in a different extent. Fabrics coated with poly(p-phenylenediamine) present higher conductivity, rather due to its polymerized structure than to the amount of polymer produced by enzyme catalysis. Herein a green approach was presented to produce polyphenols with increased fixation onto different textile substrates. These substrates reach high levels of colouration and good fastness behaviour after washing.

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Section: "In Situ" Colouration Of Fabricssupporting

confidence: 92%

Section: Introductionmentioning

confidence: 92%

Section: Catechol and P-phenylenediamine Polymerizationmentioning

confidence: 99%

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Coloured and low conductive fabrics by in situ laccase-catalysed polymerization

Noro

et al. 2019

Process Biochemistry

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“…From this data it was possible to infer the role of enzyme form on the polymerization degree. One can establish that using the later PEGylated laccase and Epoxy-PEGylated laccase higher DP and higher amount of poly(catechol) is obtained, confirming our previous findings (Su et al, 2018) (Table 1). The green, high-energy efficient and low cost methodology (Jonsson, 2005) applied, high-pressure homogenization, played however a crucial role on improving the polymerization of catechol.…”

Section: H Nmr Characterization Of Poly(catechol)supporting

confidence: 90%

“…In previous studies, we conducted the catechol polymerization with laccase from Myceliophthora thermophila using different apparatus, namely a water bath, an ultrasonic bath and a highpressure homogenizer (Su et al, 2018). The results obtained showed higher conversion yields and polymerization degrees when both high-energy reactors were used, compared to the water bath reactor.…”

Section: Introductionmentioning

confidence: 99%

Enzymatic polymerization of catechol under high-pressure homogenization for the green coloration of textiles

Noro

et al. 2018

Journal of Cleaner Production

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a b s t r a c tLaccase from Myceliophthora thermophila was used to catalyze the polymerization of catechol under high-pressure homogenization for the green coloration of textile substrates. The oxidation reactions were conducted using different forms of laccase, namely native laccase, PEGylated laccase and PEGylated laccase immobilized onto an epoxy resin. The three enzyme forms were deposited inside a polyester fabric bag during the experiments. The amount of polymer obtained was similar when using the three enzyme forms and its dispersion in water/DMSO mixture lead to powder particles of about 30e60 nm. The immobilized and PEGylated enzymes lead to poly(catechol) with 13 and 10 units, respectively, while the native form gave rise to shorter polymers (DP ¼ 8). We have shown that the oxidation of catechol conducted under high-pressure homogenization can be an efficient methodology for the in situ coloration of textiles. The polymers produced by this methodology stained strongly the textile container, revealing this experimental set-up as a promising greener coloration/coating methodology involving milder conditions than the normally used in textile processes.

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Chemically Modified Lipase from Thermomyces lanuginosus with Enhanced Esterification and Transesterification Activities

2021

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Lipase from Thermomyces lanuginosus is one of the most explored enzymes for the esterification of several added-value industrial compounds, such as biodiesel, fragrances, and flavors. Its selectivity in these reactions is mostly related with its activity towards small alcohols. In this work, the impact of the chemical modification, with 4 dodecyl chains at its surface, was evaluated regarding its transesterification and esterification activities, comparing with the native form. Linear size-differentiated alcohols (from 1 to 20 carbons in the aliphatic chain) were used to explore for the first time the effect of the chain length in both transesterification and esterification reactions, using p-nitrophenyl palmitate and oleic acid as model compounds, respectively. The chemically modified lipase showed an outstanding improvement of its catalytic performance than the native enzyme, being this increase directly proportional to the size of the alcohols chain used as substrates. The enormous potential and remarkable versatility of this novel super catalyst was here demonstrated, where diverse types of esters, differing in their potential applications (biodiesel, cosmetics, fine chemistry), were efficiently synthesized. The produced esters were fully characterized by 1 H NMR, GC-MS, and FTIR.

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The effect of high-energy environments on the structure of laccase-polymerized poly(catechol)

Cited by 23 publications

References 37 publications

Coloured and low conductive fabrics by in situ laccase-catalysed polymerization

Coloured and low conductive fabrics by in situ laccase-catalysed polymerization

Enzymatic polymerization of catechol under high-pressure homogenization for the green coloration of textiles

Chemically Modified Lipase from Thermomyces lanuginosus with Enhanced Esterification and Transesterification Activities

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