Cation–π and hydrophobic interaction controlled PET recognition in double mutated cutinase – identification of a novel binding subsite for better catalytic activity

James, Anjima; De, Susmita

doi:10.1039/d2ra03394a

Cited by 4 publications

(3 citation statements)

References 80 publications

(118 reference statements)

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“…New advances in protein engineering permit the design of novel microbial enzyme consortia with improved stability, catalytic activity, substrate specificity, and hydrolytic activity toward PET. This approach could quickly alleviate the ever-increasing microplastics and plastics in the environment [ 124 , 158 , 159 ], given the long-life expectancy of plastics [ 30 ]. This reduces the microplastic bioaccumulation in the food chain, thereby reducing medical costs while providing a safer, more cost-effective measure of environmental clean-up.…”

Section: Conclusion and Future Prospectsmentioning

confidence: 99%

An Overview into Polyethylene Terephthalate (PET) Hydrolases and Efforts in Tailoring Enzymes for Improved Plastic Degradation

Anuar

Huyop²,

Ur-Rehman³

et al. 2022

IJMS

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Plastic or microplastic pollution is a global threat affecting ecosystems, with the current generation reaching as much as 400 metric tons per/year. Soil ecosystems comprising agricultural lands act as microplastics sinks, though the impact could be unexpectedly more far-reaching. This is troubling as most plastic forms, such as polyethylene terephthalate (PET), formed from polymerized terephthalic acid (TPA) and ethylene glycol (EG) monomers, are non-biodegradable environmental pollutants. The current approach to use mechanical, thermal, and chemical-based treatments to reduce PET waste remains cost-prohibitive and could potentially produce toxic secondary pollutants. Thus, better remediation methods must be developed to deal with plastic pollutants in marine and terrestrial environments. Enzymatic treatments could be a plausible avenue to overcome plastic pollutants, given the near-ambient conditions under which enzymes function without the need for chemicals. The discovery of several PET hydrolases, along with further modification of the enzymes, has considerably aided efforts to improve their ability to degrade the ester bond of PET. Hence, this review emphasizes PET-degrading microbial hydrolases and their contribution to alleviating environmental microplastics. Information on the molecular and degradation mechanisms of PET is also highlighted in this review, which might be useful in the future rational engineering of PET-hydrolyzing enzymes.

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Section: Conclusion and Future Prospectsmentioning

confidence: 99%

An Overview into Polyethylene Terephthalate (PET) Hydrolases and Efforts in Tailoring Enzymes for Improved Plastic Degradation

Anuar

Huyop²,

Ur-Rehman³

et al. 2022

IJMS

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show abstract

“…14,40,[48][49][50][51] However, the dynamics of the binding process, which is composed of the flexibility of the binding site itself and the PET as well as the process of PET entry into the active site, cannot be adequately described by these methods, yet they have been suggested to be important factors for PET complexation and thus degradation. 4,48,49,[52][53][54] To fill this knowledge gap, we performed thorough computational simulations in combination with experimental studies on two metagenome-derived thermophilic PET hydrolases, LCC (catalytic triad: S165, D210, H242) and PES-H1 (catalytic triad: S130, D176, H208).…”

Section: Introductionmentioning

confidence: 99%

From Bulk to Binding: Decoding the Entry of PET into Hydrolase Binding Pockets

Jäckering,

Göttsch,

Schäffler

et al. 2024

Preprint

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Plastic-degrading enzymes hold promise for biocatalytic recycling of poly(ethylene terephthalate) (PET), a key synthetic polymer. Despite their potential, the current activity of PET hydrolases is not sufficient for industrial use. To unlock their full potential, a deep mechanistic understanding followed by protein engineering is required. Using cutting-edge molecular dynamics simulations and free energy analysis methods, we uncover the entire pathway from the initial binding of two PET hydrolases - the thermophilic leaf-branch compost cutinase (LCC) and polyester hydrolase 1 (PES-H1) - to an amorphous PET material to a PET chain entering the active site and adopting a hydrolyzable geometry. Our results reveal the initial PET binding and elucidate its non specific nature driven by electrostatic and hydrophobic forces. Upon PET entry into the active site, we uncover that this process can occur via one of three key pathways and detect barriers to it arising from both PET-PET and PET-enzyme interactions, with specific residues identified by in silico and in vitro mutagenesis. These insights not only advance our understanding of PET degradation mechanisms and pave the way for targeted enzyme enhancement strategies, but also offer an innovative approach applicable to enzyme studies across disciplines.

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“…PET-degrading enzymes must bind to PET, in order to cause its degradation. Therefore, such enzymes are required to possess substantial surface hydrophobicity (as well as some surface charge), 17,18,21,22 in order to engage in non-specific hydrophobic (and some cation-pi) interactions with PET. The catalytically-active sites of PET-degrading enzymes are also ringed by hydrophobic residues that help them in associating with PET chain backbones and PET's aromatic terephthalate moieties.…”

Section: Introductionmentioning

confidence: 99%

Conversion of polyethylene terephthalate into pure terephthalic acid through synergy between a solid-degrading cutinase and a reaction intermediate-hydrolysing carboxylesterase

2022

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Cation–π and hydrophobic interaction controlled PET recognition in double mutated cutinase – identification of a novel binding subsite for better catalytic activity

Abstract: Molecular recognition and binding of PET on cutinase controlled by switching between π–π and cation–π interactions.

Cited by 4 publications

References 80 publications

An Overview into Polyethylene Terephthalate (PET) Hydrolases and Efforts in Tailoring Enzymes for Improved Plastic Degradation

An Overview into Polyethylene Terephthalate (PET) Hydrolases and Efforts in Tailoring Enzymes for Improved Plastic Degradation

From Bulk to Binding: Decoding the Entry of PET into Hydrolase Binding Pockets

Conversion of polyethylene terephthalate into pure terephthalic acid through synergy between a solid-degrading cutinase and a reaction intermediate-hydrolysing carboxylesterase

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