Nano-immobilization of PETase enzyme for enhanced polyethylene terephthalate biodegradation

Jia, Yantao; Samak, Nadia A.; Hao, Xuemi; Chen, Zheng; Yang, Gama; Zhao, Xuhao; Mu, Tingzhen; Yang, Maohua; Xing, Jianmin

doi:10.1016/j.bej.2021.108205

Cited by 45 publications

(32 citation statements)

References 31 publications

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“…Finally, after 8 reuse, the TA/APTES-E and TA/AEAPTES-E retained 81% and 78% of their initial activity, respectively. These results indicated the excellent reusability of our immobilized enzyme compared to other studies, which achieved an activity retention of 23% after 6 cycles, 70% after 5 cycles, and 72% after 7 cycles …”

Section: Resultssupporting

confidence: 63%

“…High temperature can sharply destroy the spatial structure and active sites of the enzyme. Hence, its potential to tolerate high temperature is crucial . The thermal tolerance of the free and immobilized enzyme was determined at 60 °C.…”

Section: Resultsmentioning

confidence: 99%

“…These results indicated the excellent reusability of our immobilized enzyme compared to other studies, which achieved an activity retention of 23% after 6 cycles, 28 70% after 5 cycles, 29 and 72% after 7 cycles. 30 Furthermore, the free and immobilized enzymes were stored at 4 °C to investigate their storage stability. As depicted in Figure 3B, the TA/AEAPTES-E almost fully retained its initial activity after 17 days of storage, with only a 7% reduction in relative activity.…”

Section: Resultsmentioning

confidence: 99%

“…The pH at which the enzyme showed the highest activity was identified as the optimal pH value. To determine the optimal operating temperature of the enzyme, the temperature of 20 mL substrate solutions was modulated to be 20,25,30,35,40,45,50, and 55 °C using a water bath. Next, the activity of free and immobilized GOx was assayed in the substrate solutions at different temperatures at pH 5.0, respectively.…”

Section: Optimal Operating Ph Values and Temperaturesmentioning

confidence: 99%

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Engineering Mussel-Inspired Coating on Membranes for Green Enzyme Immobilization and Hyperstable Reuse

Dong

Tan²,

Pinelo

et al. 2022

Ind. Eng. Chem. Res.

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A mussel-inspired coating based on catecholamine chemistry can serve as a versatile platform for covalent enzyme immobilization. However, its application was limited by the weak salt/acid/alkali tolerance. To tackle this issue, three silane coupling agents were screened to construct a coating layer on a nylon membrane with tannic acid (TA) for enzyme immobilization. It was found that TA/3-aminopropyltriethoxysilane (APTES), and TA/3-(2-aminoethylamino) propyltriethoxysilane (AEAPTES) coatings had higher enzyme loading and activity than TA/3glycidyloxypropyltrimethoxysilane (KH-560), because TA/APTES and TA/ AEAPTES coatings formed more nanoparticles and thus provided more active sites for enzyme attachment (taking glucose oxidase as an example). Then, the pH tolerance of the immobilized enzyme was greatly enhanced by reinforcing the interfacial interactions of membrane−coating and coating− enzyme, which was realized by membrane pretreatment, ternary additive, and metal ions chelation posttreatment. The optimized TA/AEAPTES/tetraethoxysilane (TEOS)-Fe 3+ coating showed excellent pH stability and reusability, and the immobilized enzyme retained 82%, 83%, and 79% of its initial activity even after 7 h of incubation in buffer solutions at pH 3, 7, and 11, respectively. Such a coating layer was also evaluated for zearalenone hydrolase (ZHD) immobilization, and the immobilized ZHD exhibited boosted activity and robust reusability in the degradation of zearalenone (ZEN, a refractory and hypertoxic mycotoxin). This work not only offered a green and practical strategy for enzyme immobilization but also provided fundamental data in the design of a musselinspired coating layer toward versatile applications.

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Section: Resultssupporting

confidence: 63%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Optimal Operating Ph Values and Temperaturesmentioning

confidence: 99%

See 2 more Smart Citations

Engineering Mussel-Inspired Coating on Membranes for Green Enzyme Immobilization and Hyperstable Reuse

Dong

Tan²,

Pinelo

et al. 2022

Ind. Eng. Chem. Res.

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“…A highly interesting approach that can be applied to PET degradation technology in the future is the concept of nano-immobilization of enzymes to improve their tolerance to temperature and pH. The first attempts to use immobilized enzymes have been recently achieved successfully ( Jia et al, 2021 ). Another perspective, which should be included in the discussion, is the possibility of reuse of the products of PET degradation (such as EG and TPA) to synthesize a new PET with similar properties as a virgin PET.…”

Section: Introductionmentioning

confidence: 99%

Current Knowledge on Polyethylene Terephthalate Degradation by Genetically Modified Microorganisms

Urbanek

Kosiorowska

Mirończuk

2021

Front. Bioeng. Biotechnol.

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The global production of polyethylene terephthalate (PET) is estimated to reach 87.16 million metric tons by 2022. After a single use, a remarkable part of PET is accumulated in the natural environment as plastic waste. Due to high hydrophobicity and high molecular weight, PET is hardly biodegraded by wild-type microorganisms. To solve the global problem of uncontrolled pollution by PET, the degradation of plastic by genetically modified microorganisms has become a promising alternative for the plastic circular economy. In recent years many studies have been conducted to improve the microbial capacity for PET degradation. In this review, we summarize the current knowledge about metabolic engineering of microorganisms and protein engineering for increased biodegradation of PET. The focus is on mutations introduced to the enzymes of the hydrolase class—PETase, MHETase and cutinase—which in the last few years have attracted growing interest for the PET degradation processes. The modifications described in this work summarize the results obtained so far on the hydrolysis of polyethylene terephthalate based on the released degradation products of this polymer.

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Enzyme-Assisted Biodegradation of Micro-Nanoplastics: Advances and Future Outlook on the Management of Plastic Pollution

Dhanasekaran,

Krishnan

2024

Management of Micro and Nano-Plastics in Soil and Biosolids

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Nano-immobilization of PETase enzyme for enhanced polyethylene terephthalate biodegradation

Cited by 45 publications

References 31 publications

Engineering Mussel-Inspired Coating on Membranes for Green Enzyme Immobilization and Hyperstable Reuse

Engineering Mussel-Inspired Coating on Membranes for Green Enzyme Immobilization and Hyperstable Reuse

Current Knowledge on Polyethylene Terephthalate Degradation by Genetically Modified Microorganisms

Enzyme-Assisted Biodegradation of Micro-Nanoplastics: Advances and Future Outlook on the Management of Plastic Pollution

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