Overexpression and kinetic analysis of Ideonella sakaiensis PETase for polyethylene terephthalate (PET) degradation

Aer, Lizhu; Jiang, Qifa; Gul, Ijaz; Qi, Zixuan; Feng, Juan; Tang, Lin

doi:10.1016/j.envres.2022.113472

Cited by 15 publications

(6 citation statements)

References 58 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…genes to boost its survival capability in habitats, such as soil and water. Authors have demonstrated that PETase could be successfully expressed in Chlamydomonas reinhardtii and Escherichia coli , respectively (Aer et al 2022 ; Kim et al 2020 ; Shi et al 2021 ). Others (e.g., (Ma et al 2018 ; Son et al 2019 ; Meng et al 2021 )) have screened PETase mutants and variants to improve enzymatic performance as well as thermal stability.…”

Section: Discussionmentioning

confidence: 99%

“…Although PET is recyclable, high percentages of plastic waste accumulate in the ecosystems, causing a severe environmental burden, which is mostly undiscovered (Wallace et al 2020 ; Prata et al 2019 ; Chen et al 2018 ). Hence, plastic degradation is one of the major global challenges, which have to be tackled urgently (Aer et al 2022 ).…”

Section: Introductionmentioning

confidence: 99%

“…This Gram-negative strain reveals optimal growth rates at pH 7–7.5 and temperatures of 30–37 °C (Tanasupawat et al 2016 ). Two key enzymes could be identified, both facilitating the degradation and assimilation of PET: the exo-enzyme PETase converts PET to mono-(2-hydroxyethyl) terephthalate (MHET) with a relatively high activity at room temperature, when compared to other PET-degrading enzymes (Aer et al 2022 ). Then, in the cell periplasm, MHETase hydrolyzes MHET to the PET educts ethylene glycol (EG) and terephthalic acid (TPA), which is subsequently transported into the cytoplasm and introduced into the tricarboxylic acid cycle (Palm et al 2019 ).…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Biodegradation of different PET variants from food containers by Ideonella sakaiensis

et al. 2022

View full text Add to dashboard Cite

The accumulation of macro-, micro- and nano-plastic wastes in the environment is a major global concern, as these materials are resilient to degradation processes. However, microorganisms have evolved their own biological means to metabolize these petroleum-derived polymers, e.g., Ideonella sakaiensis has recently been found to be capable of utilizing polyethylene terephthalate (PET) as its sole carbon source. This study aims to prove its potential capacity to biodegrade two commercial PET materials, obtained from food packaging containers. Plastic pieces of different crystallinity were simultaneously introduced to Ideonella sakaiensis during a seven-week lasting investigation. Loss in weight, appearance of plastics, as well as growth of Ideonella sakaiensis—through quantitative real-time PCR—were determined. Both plastics were found enzymatically attacked in a two-stage degradation process, reaching biodegradation capacities of up to 96%. Interestingly, the transparent, high crystallinity PET was almost fully degraded first, followed by the colored low-crystallinity PET. Results of quantitative real-time PCR-based gene copy numbers were found in line with experimental results, thus underlining its potential of this method to be applied in future studies with Ideonella sakaiensis.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Biodegradation of different PET variants from food containers by Ideonella sakaiensis

et al. 2022

View full text Add to dashboard Cite

show abstract

“…Escherichia coli intracellular expression is one of the most commonly used technique in laboratory due to low cost and ease of manipulation, but further applications with this system are hampered by additional protein purification processes. Secreted expression in E. coli involving signal peptide optimization and chaperon co-expression was thus exploited for Is PETase production, but the bacterial endotoxin remains a potential threat (Seo et al 2019 ; Shi et al 2021 ; Aer et al 2022 ). Other prokaryotic cell factories such as Bacillus subtilis and Pseudomonas putida have been utilized to scale up PET hydrolase production (Xi et al 2021 ; Wang et al 2020 ; Oh et al 2022 ; Huang et al 2018 ).…”

Section: Introductionmentioning

confidence: 99%

Functional tailoring of a PET hydrolytic enzyme expressed in Pichia pastoris

Shi

Huang

et al. 2023

Bioresour. Bioprocess.

View full text Add to dashboard Cite

Using enzymes to hydrolyze and recycle poly(ethylene terephthalate) (PET) is an attractive eco-friendly approach to manage the ever-increasing PET wastes, while one major challenge to realize the commercial application of enzyme-based PET degradation is to establish large-scale production methods to produce PET hydrolytic enzyme. To achieve this goal, we exploited the industrial strain Pichia pastoris to express a PET hydrolytic enzyme from Caldimonas taiwanensis termed CtPL-DM. In contrast to the protein expressed in Escherichia coli, CtPL-DM expressed in P. pastoris is inactive in PET degradation. Structural analysis indicates that a putative N-glycosylation site N181 could restrain the conformational change of a substrate-binding Trp and hamper the enzyme action. We thus constructed N181A to remove the N-glycosylation and found that the PET hydrolytic activity of this variant was restored. The performance of N181A was further enhanced via molecular engineering. These results are of valuable in terms of PET hydrolytic enzyme production in industrial strains in the future. Graphical Abstract

show abstract

“…14,[20][21][22] Studies to improve the performance of these enzymes is indeed a valuable research area. [23][24][25] In the year 2022, a novel enzyme PHL7 was discovered by Zimmermann and co-workers, which shows promising activity for large scale degradation of PET. 26,27 In the same year, application of machine learning techniques are also used to design FAST-IsPETase, 28 which shows higher activity.…”

Section: Introductionmentioning

confidence: 99%

Cation–π and hydrophobic interaction controlled PET recognition in double mutated cutinase – identification of a novel binding subsite for better catalytic activity

James

2022

RSC Adv.

View full text Add to dashboard Cite

show abstract

Overexpression and kinetic analysis of Ideonella sakaiensis PETase for polyethylene terephthalate (PET) degradation

Cited by 15 publications

References 58 publications

Biodegradation of different PET variants from food containers by Ideonella sakaiensis

Biodegradation of different PET variants from food containers by Ideonella sakaiensis

Functional tailoring of a PET hydrolytic enzyme expressed in Pichia pastoris

Cation–π and hydrophobic interaction controlled PET recognition in double mutated cutinase – identification of a novel binding subsite for better catalytic activity

Contact Info

Product

Resources

About