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@article{1863383,
author = {Wei, Ren and von Haugwit, Gerlis and Pfaff, Lara and Mičan, Jan and Badenhorst, Christoffel P. S. and Liu, Weidong and Weber, Gert and Austin, Harry P. and Bednář, David and Damborský, Jiří and Bornscheuer, Uwe T.},
article_number = {6},
doi = {http://dx.doi.org/10.1021/acscatal.1c05856},
keywords = {Hydrolase; enzymatic degradation; interfacial biocatalysis; plastic recycling; protein engineering; polyethylene terephthalate (PET); product inhibition; thermostability},
language = {eng},
issn = {2155-5435},
journal = {ACS Catalysis},
title = {Mechanism-Based Design of Efficient PET Hydrolases},
url = {https://pubs.acs.org/doi/10.1021/acscatal.1c05856},
volume = {12},
year = {2022}
}
TY - JOUR
ID - 1863383
AU - Wei, Ren - von Haugwit, Gerlis - Pfaff, Lara - Mičan, Jan - Badenhorst, Christoffel P. S. - Liu, Weidong - Weber, Gert - Austin, Harry P. - Bednář, David - Damborský, Jiří - Bornscheuer, Uwe T.
PY - 2022
TI - Mechanism-Based Design of Efficient PET Hydrolases
JF - ACS Catalysis
VL - 12
IS - 6
SP - 3382-3396
EP - 3382-3396
PB - American Chemical Society
SN - 21555435
KW - Hydrolase
KW - enzymatic degradation
KW - interfacial biocatalysis
KW - plastic recycling
KW - protein engineering
KW - polyethylene terephthalate (PET)
KW - product inhibition
KW - thermostability
UR - https://pubs.acs.org/doi/10.1021/acscatal.1c05856
N2 - Polyethylene terephthalate (PET) is the most widespread synthetic polyester, having been utilized in textile fibers and packaging materials for beverages and food, contributing considerably to the global solid waste stream and environmental plastic pollution. While enzymatic PET recycling and upcycling have recently emerged as viable disposal methods for a circular plastic economy, only a handful of benchmark enzymes have been thoroughly described and subjected to protein engineering for improved properties over the last 16 years. By analyzing the specific material properties of PET and the reaction mechanisms in the context of interfacial biocatalysis, this Perspective identifies several limitations in current enzymatic PET degradation approaches. Unbalanced enzyme-substrate interactions, limited thermostability, and low catalytic efficiency at elevated reaction temperatures, and inhibition caused by oligomeric degradation intermediates still hamper industrial applications that require high catalytic efficiency. To overcome these limitations, successful protein engineering studies using innovative experimental and computational approaches have been published extensively in recent years in this thriving research field and are summarized and discussed in detail here. The acquired knowledge and experience will be applied in the near future to address plastic waste contributed by other mass-produced polymer types (e.g., polyamides and polyurethanes) that should also be properly disposed by biotechnological approaches.
ER -
WEI, Ren, Gerlis VON HAUGWIT, Lara PFAFF, Jan MIČAN, Christoffel P. S. BADENHORST, Weidong LIU, Gert WEBER, Harry P. AUSTIN, David BEDNÁŘ, Jiří DAMBORSKÝ and Uwe T. BORNSCHEUER. Mechanism-Based Design of Efficient PET Hydrolases. \textit{ACS Catalysis}. American Chemical Society, 2022, vol.~12, No~6, p.~3382-3396. ISSN~2155-5435. Available from: https://dx.doi.org/10.1021/acscatal.1c05856.
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