Insight on recently discovered PET polyester‑degrading enzymes, thermostability and activity analyses

The flexibility and the low production costs offered by plastics have made them crucial to society. Unfortunately, due to their resistance to biological degradation, plastics remain in the environment for an extended period of time, posing a growing risk to life on earth. Synthetic treatments of pla...

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Main Authors: Leow, Adam Thean Chor, Mohd Yahaya, Normi, Mohd Shariff, Fairolniza, Bataiya, Sunusi Buhari, Nezhad, Nima Ghahremani
Format: Article
Language:English
Published: SpringerOpen 2024
Online Access:http://psasir.upm.edu.my/id/eprint/117716/
http://psasir.upm.edu.my/id/eprint/117716/1/117716.pdf
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author Leow, Adam Thean Chor
Mohd Yahaya, Normi
Mohd Shariff, Fairolniza
Bataiya, Sunusi Buhari
Nezhad, Nima Ghahremani
author_facet Leow, Adam Thean Chor
Mohd Yahaya, Normi
Mohd Shariff, Fairolniza
Bataiya, Sunusi Buhari
Nezhad, Nima Ghahremani
author_sort Leow, Adam Thean Chor
building UPM Institutional Repository
collection Online Access
description The flexibility and the low production costs offered by plastics have made them crucial to society. Unfortunately, due to their resistance to biological degradation, plastics remain in the environment for an extended period of time, posing a growing risk to life on earth. Synthetic treatments of plastic waste damage the environment and may cause damage to human health. Bacterial and fungal isolates have been reported to degrade plastic polymers in a logistic safe approach with the help of their microbial cell enzymes. Recently, the bacterial strain Ideonella sakaiensis (201-F6) was discovered to break down and assimilate polyethylene terephthalate (PET) plastic via metabolic processes at 30 °C to 37 °C. PETase and MHETase enzymes help the bacterium to accomplish such tremendous action at lower temperatures than previously discovered enzymes. In addition to functioning at low temperatures, the noble bacterium's enzymes have amazing qualities over pH and PET plastic degradation, including a shorter period of degradation. It has been proven that using the enzyme PETase, this bacterium hydrolyzes the ester linkages of PET plastic, resulting in production of terephthalic acid (TPA), nontoxic compound and mono-2-hydroxyethyl (MHET), along with further depolymerization of MHET to release ethylene glycogen (EG) and terephthalic acid (TPA) by the second enzyme MHETase. Enzymatic plastic degradation has been proposed as an environmentally friendly and long-term solution to plastic waste in the environment. As a result, this review focuses on the enzymes involved in hydrolyzing PET plastic polymers, as well as some of the other microorganisms involved in plastic degradation.
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spelling upm-1177162025-07-10T02:15:52Z http://psasir.upm.edu.my/id/eprint/117716/ Insight on recently discovered PET polyester‑degrading enzymes, thermostability and activity analyses Leow, Adam Thean Chor Mohd Yahaya, Normi Mohd Shariff, Fairolniza Bataiya, Sunusi Buhari Nezhad, Nima Ghahremani The flexibility and the low production costs offered by plastics have made them crucial to society. Unfortunately, due to their resistance to biological degradation, plastics remain in the environment for an extended period of time, posing a growing risk to life on earth. Synthetic treatments of plastic waste damage the environment and may cause damage to human health. Bacterial and fungal isolates have been reported to degrade plastic polymers in a logistic safe approach with the help of their microbial cell enzymes. Recently, the bacterial strain Ideonella sakaiensis (201-F6) was discovered to break down and assimilate polyethylene terephthalate (PET) plastic via metabolic processes at 30 °C to 37 °C. PETase and MHETase enzymes help the bacterium to accomplish such tremendous action at lower temperatures than previously discovered enzymes. In addition to functioning at low temperatures, the noble bacterium's enzymes have amazing qualities over pH and PET plastic degradation, including a shorter period of degradation. It has been proven that using the enzyme PETase, this bacterium hydrolyzes the ester linkages of PET plastic, resulting in production of terephthalic acid (TPA), nontoxic compound and mono-2-hydroxyethyl (MHET), along with further depolymerization of MHET to release ethylene glycogen (EG) and terephthalic acid (TPA) by the second enzyme MHETase. Enzymatic plastic degradation has been proposed as an environmentally friendly and long-term solution to plastic waste in the environment. As a result, this review focuses on the enzymes involved in hydrolyzing PET plastic polymers, as well as some of the other microorganisms involved in plastic degradation. SpringerOpen 2024 Article PeerReviewed text en http://psasir.upm.edu.my/id/eprint/117716/1/117716.pdf Leow, Adam Thean Chor and Mohd Yahaya, Normi and Mohd Shariff, Fairolniza and Bataiya, Sunusi Buhari and Nezhad, Nima Ghahremani (2024) Insight on recently discovered PET polyester‑degrading enzymes, thermostability and activity analyses. 3 Biotech, 14. art. no. 31. pp. 1-16. ISSN 2190-572X; eISSN: 2190-5738 https://link.springer.com/article/10.1007/s13205-023-03882-8 10.1007/s13205-023-03882-8
spellingShingle Leow, Adam Thean Chor
Mohd Yahaya, Normi
Mohd Shariff, Fairolniza
Bataiya, Sunusi Buhari
Nezhad, Nima Ghahremani
Insight on recently discovered PET polyester‑degrading enzymes, thermostability and activity analyses
title Insight on recently discovered PET polyester‑degrading enzymes, thermostability and activity analyses
title_full Insight on recently discovered PET polyester‑degrading enzymes, thermostability and activity analyses
title_fullStr Insight on recently discovered PET polyester‑degrading enzymes, thermostability and activity analyses
title_full_unstemmed Insight on recently discovered PET polyester‑degrading enzymes, thermostability and activity analyses
title_short Insight on recently discovered PET polyester‑degrading enzymes, thermostability and activity analyses
title_sort insight on recently discovered pet polyester‑degrading enzymes, thermostability and activity analyses
url http://psasir.upm.edu.my/id/eprint/117716/
http://psasir.upm.edu.my/id/eprint/117716/
http://psasir.upm.edu.my/id/eprint/117716/
http://psasir.upm.edu.my/id/eprint/117716/1/117716.pdf