The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Rational Protein Engineering of Thermo-Stable PETase from Ideonella sakaiensis for Highly Efficient PET Degradation
Abstract
Widespread utilization of polyethylene terephthalate (PET) has caused a variety of environmental and health problems; thus, the enzymatic degradation of PET can be a promising solution. Although PETase from Ideonalla sakaiensis ( Is PETase) has been reported to have the highest PET degradation activity under mild conditions of all PET-degrading enzymes reported to date, its low thermal stability limits its ability for efficient and practical enzymatic degradation of PET. Using the structural information on Is PETase, we developed a rational protein engineering strategy using several Is PETase variants that were screened for high thermal stability to improve PET degradation activity. In particular, the Is PETase S121E/D186H/R280A variant, which was designed to have a stabilized β6-β7 connecting loop and extended subsite IIc, had a T m value that was increased by 8.81 °C and PET degradation activity was enhanced by 14-fold at 40 °C in comparison with Is PETase WT . The designed structural modifications were further verified through structure determination of the variants, and high thermal stability was further confirmed by a heat-inactivation experiment. The proposed strategy and developed variants represent an important advancement for achieving the complete biodegradation of PET under mild conditions.
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A bacterium that degrades and assimilates poly(ethylene terephthalate)
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Microplastic contamination of river beds significantly reduced by catchment-wide flooding
Hurley, R., Woodward, J., & Rothwell, J. J. (2018) · Nature Geoscience · doi:10.1038/s41561-018-0080-1 · Cited by 1,003
Chemical Recycling of Poly(ethylene terephthalate)
Paszun, D., & Spychaj, T. (1997) · Industrial & Engineering Chemistry Research · doi:10.1021/ie960563c · Cited by 661
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Metadata
- Authors
- Son, H. F., Cho, I. J., Joo, S., Seo, H., Sagong, H.-Y., Choi, S. Y., Lee, S. Y., & Kim, K.-J.
- Venue
- ACS Catalysis
- Publisher
- American Chemical Society (ACS)
- Published
- 2019-03-11
- Volume
- 9
- Issue
- 4
- Pages
- 3519-3526
- ISSN
- 2155-5435 (ISSN-L)
- OpenAlex
- W2922444498
- Cited by
- 572
- References
- 3
- FWCI
- 12.03
- Type
- journal article
- Language
- en
- Open access
- closed
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