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Enhanced biodegradation of waste poly(ethylene terephthalate) using a reinforced plastic degrading enzyme complex

Authors
Hwang, D.-H.Lee, M.-E.Cho, B.-H.Oh, J.W.You, S.K.Ko, Y.J.Hyeon, J.E.Han, S.O.
Issue Date
10월-2022
Publisher
Elsevier B.V.
Keywords
Binding affinity; Carboxylic ester hydrolases complex; Enzyme stability; Sequential degradation; Waste poly (ethylene terephthalate)
Citation
Science of the Total Environment, v.842
Indexed
SCIE
SCOPUS
Journal Title
Science of the Total Environment
Volume
842
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/143571
DOI
10.1016/j.scitotenv.2022.156890
ISSN
0048-9697
Abstract
Poly(ethylene terephthalate) (PET) is synthesized via a rich ester bond between terephthalate (TPA) and ethylene glycol (EG). Because of this, PET degradation takes a long time and PET accumulates in the environment. Many studies have been conducted to improve PET degrading enzyme to increase the efficiency of PET depolymerization. However, enzymatic PET decomposition is still restricted, making upcycling and recycling difficult. Here, we report a novel PET degrading complex composed of Ideonella sakaiensis PETase and Candida antarctica lipase B (CALB) that improves degradability, binding ability and enzyme stability. The reaction mechanism of chimeric PETase (cPETase) and chimeric CALB (cCALB) was confirmed by PET and bis (2-hydroxyethyl terephthalate) (BHET). cPETase generated BHET and mono (2-hydroxyethyl terephthalate (MHET) and cCALB produced terephthalate (TPA). Carbohydrate binding module 3 (CBM3) in the scaffolding protein greatly improved PET film binding affinity. Finally, the final enzyme complex demonstrated a 6.5-fold and 8.0-fold increase in the efficiency of hydrolysis from PET with either high crystalline or waste to TPA than single enzymes, respectively. This complex could effectively break down waste PET while maintaining enzyme stability and would be applied for biological upcycling of TPA. © 2022 Elsevier B.V.
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