2021
DOI: 10.1016/j.biotechadv.2021.107811
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A comprehensive and critical review on key elements to implement enzymatic PET depolymerization for recycling purposes

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Cited by 83 publications
(85 citation statements)
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“…These biocatalytic reactions have the advantage of enabling PET hydrolysis under mild conditions (30-75 °C and ambient pressure) in aqueous solutions to provide BHET, mono-2hydroxyethylterephthalate (MHET), TPA, and EG with varying selectivity as products (Figure 45). Many reviews have been written on this topic 21,681,[785][786][787][788][789][790] and it is a highly active area of research, thus we only discuss highlights here. The first report of enzymatic hydrolysis of PET was in 2005 from Müller et al 791 wherein they showed appreciable extents of PET conversion over 3 weeks at 55 °C using a cutinase enzyme from the thermophilic bacterium Thermobifida fusca.…”
Section: Biocatalysismentioning
confidence: 99%
“…These biocatalytic reactions have the advantage of enabling PET hydrolysis under mild conditions (30-75 °C and ambient pressure) in aqueous solutions to provide BHET, mono-2hydroxyethylterephthalate (MHET), TPA, and EG with varying selectivity as products (Figure 45). Many reviews have been written on this topic 21,681,[785][786][787][788][789][790] and it is a highly active area of research, thus we only discuss highlights here. The first report of enzymatic hydrolysis of PET was in 2005 from Müller et al 791 wherein they showed appreciable extents of PET conversion over 3 weeks at 55 °C using a cutinase enzyme from the thermophilic bacterium Thermobifida fusca.…”
Section: Biocatalysismentioning
confidence: 99%
“…The enzyme’s family of cutinases, lipases, proteases, and esterases are repurposed from original biopolymer degradation to corresponding bonds containing C-X class of plastic types (Carniel et al ., 2021; Satti & Shah, 2020). The PE, PS, LDPE, and PVA are only C-C class of plastic types in the local enzyme database associated with less than 20% of overall unique ids in the database.…”
Section: Resultsmentioning
confidence: 99%
“…This enzyme group also serves as a representative set of catalysts to be further rened by evolution or engineering approaches for biotechnological application. 52,53,55,56 Though not pursued here, the exibility and throughput of this assay would be ideal for use comparing the activity of wild-type enzymes to such a panel of mutants against native or non-native substrates. Additionally, we examined commercial esterases, which may better simulate the type of highly diverse enzyme sets obtained in a library screen or an environmental sample.…”
Section: Discussionmentioning
confidence: 99%