Structural and functional studies of a Fusarium oxysporum cutinase with polyethylene terephthalate modification potential

Dimarogona, Maria; Nikolaivits, Efstratios; Kanelli, Maria; Christakopoulos, Paul; Sandgren, Mats; Topakas, Evangelos

doi:10.1016/j.bbagen.2015.08.009

Cited by 75 publications

(71 citation statements)

References 75 publications

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“…10 been reported previously [14]. In this case, a large enzyme amount is detected in the culture medium at both induction temperatures (64% and 41% at 37 ο C and 16 ο C, respectively).…”

Section: A C C E P T E D Accepted Manuscriptmentioning

confidence: 61%

“…The gene cut5a from the mesophilic fungus F. oxysporum, encoding the respective cutinase, had already been expressed in a soluble form in E. coli BL21 cells [14]. Although the recombinant enzyme was active, it exhibited very low tolerance in temperature, losing most of its activity after 2 h incubation at 35 ο C. In this study, we report the functional expression of the same gene in E. coli Origami 2 strain, using two expression strategies, in order to produce an active, soluble and stable product.…”

Section: Discussionmentioning

confidence: 99%

“…For both, the highest catalytic efficiency (k cat /K M ) is presented for the C 4 ester (pNPB), but in the case of the BL21 product [14] that value is 16 times higher than for the Origami product. In all three substrates tested, the catalytic efficiency of the Origami-produced cutinase was lower than the respective one from the BL21 cells.…”

Section: Accepted Manuscriptmentioning

confidence: 93%

“…Two different E. coli strains were used for the expression of the F. oxysporum constructed, as described previously [14]. The utilization or not of a pelB signal sequence determined periplasmic or cytoplasmic expression of the recombinant enzyme, respectively.…”

Section: Strains and Vectorsmentioning

confidence: 99%

“…Structure of FoCut5a cutinase showing the two disulphide bonds that stabilize the tertiary structure[14].…”

mentioning

confidence: 99%

See 4 more Smart Citations

Microbial host selection and periplasmic folding in Escherichia coli affect the biochemical characteristics of a cutinase from Fusarium oxysporum

Nikolaivits

Kokkinou

Karpusas

2016

Protein Expression and Purification

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“…10 been reported previously [14]. In this case, a large enzyme amount is detected in the culture medium at both induction temperatures (64% and 41% at 37 ο C and 16 ο C, respectively).…”

Section: A C C E P T E D Accepted Manuscriptmentioning

confidence: 61%

Section: Discussionmentioning

confidence: 99%

Section: Accepted Manuscriptmentioning

confidence: 93%

Section: Strains and Vectorsmentioning

confidence: 99%

“…Structure of FoCut5a cutinase showing the two disulphide bonds that stabilize the tertiary structure[14].…”

mentioning

confidence: 99%

See 3 more Smart Citations

Microbial host selection and periplasmic folding in Escherichia coli affect the biochemical characteristics of a cutinase from Fusarium oxysporum

Nikolaivits

Kokkinou

Karpusas

2016

Protein Expression and Purification

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Exploring the substrate spectrum of phylogenetically distinct bacterial polyesterases

Makryniotis,

Nikolaivits,

Taxeidis

et al. 2024

Biotechnology Journal

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The rapid escalation of plastic waste accumulation presents a significant threat of the modern world, demanding an immediate solution. Over the last years, utilization of the enzymatic machinery of various microorganisms has emerged as an environmentally friendly asset in tackling this pressing global challenge. Thus, various hydrolases have been demonstrated to effectively degrade polyesters. Plastic waste streams often consist of a variety of different polyesters, as impurities, mainly due to wrong disposal practices, rendering recycling process challenging. The elucidation of the selective degradation of polyesters by hydrolases could offer a proper solution to this problem, enhancing the recyclability performance. Towards this, our study focused on the investigation of four bacterial polyesterases, including DaPUase, IsPETase, PfPHOase, and Se1JFR, a novel PETase‐like lipase. The enzymes, which were biochemically characterized and structurally analyzed, demonstrated degradation ability of synthetic plastics. While a consistent pattern of polyesters’ degradation was observed across all enzymes, Se1JFR stood out in the degradation of PBS, PLA, and polyether PU. Additionally, it exhibited comparable results to IsPETase, a benchmark mesophilic PETase, in the degradation of PCL and semi‐crystalline PET. Our results point out the wide substrate spectrum of bacterial hydrolases and underscore the significant potential of PETase‐like enzymes in polyesters degradation.

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Ionic Liquids as Extractants for Nanoplastics

2020

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Plastic waste in the ocean and on land in the form of nanoplastics is endangering food and drinking water supplies, raising the need for new strategies for the removal of plastic nanoparticles from complex media. In the present contribution we suggest considering ionic liquids as extractants, since they show several advantageous properties that may facilitate the design of efficient separation processes. Through varying the anion and the side chain at the cation, the interactions between the extractant and the polymer can be strengthened and tuned, and thereby the disintegration of the particle into separate polymer chains can be controlled. Oxidized moieties can also be efficiently solvated, given the amphiphilic nature of the considered ionic liquids, allowing also realistic particles to be extracted into these solvents. The phase transfer was found to be thermodynamically and kinetically possible, which is supported by the complicated structure of the ionic liquid-water interface through the rearrangement of the interfacial ions, and the formation of a micelle around the plastic already at the edge of the aqueous phase.

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Structural and functional studies of a Fusarium oxysporum cutinase with polyethylene terephthalate modification potential

Cited by 75 publications

References 75 publications

Microbial host selection and periplasmic folding in Escherichia coli affect the biochemical characteristics of a cutinase from Fusarium oxysporum

Microbial host selection and periplasmic folding in Escherichia coli affect the biochemical characteristics of a cutinase from Fusarium oxysporum

Exploring the substrate spectrum of phylogenetically distinct bacterial polyesterases

Ionic Liquids as Extractants for Nanoplastics

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