PETase gets hot

Maria Joscelind Alvina; Jingjing Wei; Fei Sun

doi:10.1016/j.checat.2022.09.033

PETase gets hot

Maria Joscelind Alvina
, Jingjing Wei^*
, Fei Sun^*

^*Corresponding author for this work

Department of Chemical and Biological Engineering

Research output: Contribution to journal › Comment/debate

Abstract

Few enzymes thus far can effectively deconstruct real-world plastic products comprising highly crystalline polyethylene terephthalate (PET). Recently in Nature Catalysis, Bell et al. developed a directed evolution platform for PETase engineering, generating a robust, thermally stable biocatalyst, HotPETase, capable of decomposing untreated PET samples (up to ∼41% crystallinity).

Original language	English
Pages (from-to)	2437-2439
Number of pages	3
Journal	Chem Catalysis
Volume	2
Issue number	10
DOIs	https://doi.org/10.1016/j.checat.2022.09.033
Publication status	Published - 20 Oct 2022

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© 2022 Elsevier Inc.

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10.1016/j.checat.2022.09.033

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@article{b33c9b419770496d826d5dbc6c31d98b,

title = "PETase gets hot",

abstract = "Few enzymes thus far can effectively deconstruct real-world plastic products comprising highly crystalline polyethylene terephthalate (PET). Recently in Nature Catalysis, Bell et al. developed a directed evolution platform for PETase engineering, generating a robust, thermally stable biocatalyst, HotPETase, capable of decomposing untreated PET samples (up to ∼41\% crystallinity).",

author = "Alvina, \{Maria Joscelind\} and Jingjing Wei and Fei Sun",

note = "Publisher Copyright: {\textcopyright} 2022 Elsevier Inc.",

year = "2022",

month = oct,

day = "20",

doi = "10.1016/j.checat.2022.09.033",

language = "English",

volume = "2",

pages = "2437--2439",

journal = "Chem Catalysis",

issn = "2667-1107",

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TY - JOUR

T1 - PETase gets hot

AU - Alvina, Maria Joscelind

AU - Wei, Jingjing

AU - Sun, Fei

PY - 2022/10/20

Y1 - 2022/10/20

N2 - Few enzymes thus far can effectively deconstruct real-world plastic products comprising highly crystalline polyethylene terephthalate (PET). Recently in Nature Catalysis, Bell et al. developed a directed evolution platform for PETase engineering, generating a robust, thermally stable biocatalyst, HotPETase, capable of decomposing untreated PET samples (up to ∼41% crystallinity).

AB - Few enzymes thus far can effectively deconstruct real-world plastic products comprising highly crystalline polyethylene terephthalate (PET). Recently in Nature Catalysis, Bell et al. developed a directed evolution platform for PETase engineering, generating a robust, thermally stable biocatalyst, HotPETase, capable of decomposing untreated PET samples (up to ∼41% crystallinity).

UR - https://www.webofscience.com/wos/woscc/full-record/WOS:000901459800017

UR - https://openalex.org/W4306956430

U2 - 10.1016/j.checat.2022.09.033

DO - 10.1016/j.checat.2022.09.033

M3 - Comment/debate

SN - 2667-1107

VL - 2

SP - 2437

EP - 2439

JO - Chem Catalysis

JF - Chem Catalysis

IS - 10

ER -

PETase gets hot

Abstract

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