Modulation ofIdeonella sakaiensisPETase active site flexibility and activity on morphologically distinct substrates by surface charge engineering Article Swipe
Ke Ding
,
Zarina Levitskaya
,
Barindra Sana
,
Rupali Reddy Pasula
,
Srinivasaraghavan Kannan
,
A. Adam
,
Vishnu Vadanan Sundaravadanam
,
Chandra Verma
,
Sierin Lim
,
Farid J. Ghadessy
·
YOU?
·
· 2024
· Open Access
·
· DOI: https://doi.org/10.1101/2024.05.07.589851
YOU?
·
· 2024
· Open Access
·
· DOI: https://doi.org/10.1101/2024.05.07.589851
Enzymatic hydrolysis of polyethylene terephthalate (PET) waste is a compelling strategy for environmentally friendly recycling of a major pollutant. Here, we investigate the effects of surface charge point mutations both proximal and distal to the active site of the mesophilic PET-degrading enzyme from Ideonella sakaienses ( Is PETase) and an engineered thermostable variant with superior activity, STAR PETase. The vicinal K95A mutation significantly inhibited Is PETase activity on mechanically processed PET powder. Conversely, this mutation significantly increased hydrolysis of PET powder in the STAR PETase background. Activity of both enzymes on PET film was inhibited by the K95A mutation, highlighting complex interplay between mutation context and substrate morphology. Further installing the distal R132N and R280A surface charge mutations potentiated activity of STAR on all substrates tested. This variant afforded 100% degradation of bottle-grade PET powder in 3 days at 40°C reaction temperature, a 3-fold improvement over Is PETase. Molecular dynamics simulations reveal modulation of active site flexibility in mutants, which differentially impacts both hydrolysis of morphologically distinct PET substrates and the concentration-dependent inhibition phenomenon observed for PETase.
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- Type
- preprint
- Language
- en
- Landing Page
- https://doi.org/10.1101/2024.05.07.589851
- https://www.biorxiv.org/content/biorxiv/early/2024/05/10/2024.05.07.589851.full.pdf
- OA Status
- green
- Cited By
- 1
- References
- 59
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W4396829856
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Raw OpenAlex JSON
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https://openalex.org/W4396829856Canonical identifier for this work in OpenAlex
- DOI
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https://doi.org/10.1101/2024.05.07.589851Digital Object Identifier
- Title
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Modulation ofIdeonella sakaiensisPETase active site flexibility and activity on morphologically distinct substrates by surface charge engineeringWork title
- Type
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preprintOpenAlex work type
- Language
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enPrimary language
- Publication year
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2024Year of publication
- Publication date
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2024-05-10Full publication date if available
- Authors
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Ke Ding, Zarina Levitskaya, Barindra Sana, Rupali Reddy Pasula, Srinivasaraghavan Kannan, A. Adam, Vishnu Vadanan Sundaravadanam, Chandra Verma, Sierin Lim, Farid J. GhadessyList of authors in order
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https://doi.org/10.1101/2024.05.07.589851Publisher landing page
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https://www.biorxiv.org/content/biorxiv/early/2024/05/10/2024.05.07.589851.full.pdfDirect link to full text PDF
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YesWhether a free full text is available
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greenOpen access status per OpenAlex
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https://www.biorxiv.org/content/biorxiv/early/2024/05/10/2024.05.07.589851.full.pdfDirect OA link when available
- Concepts
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Context (archaeology), Active site, Mutant, Mutation, Substrate (aquarium), Enzyme, Hydrolysis, Enzyme assay, Biophysics, Surface charge, Chemistry, Materials science, Biochemistry, Biology, Gene, Physical chemistry, Ecology, PaleontologyTop concepts (fields/topics) attached by OpenAlex
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1Total citation count in OpenAlex
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2025: 1Per-year citation counts (last 5 years)
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59Number of works referenced by this work
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10Other works algorithmically related by OpenAlex
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