globalchange  > 气候变化与战略
DOI: 10.1073/pnas.1718804115
论文题名:
Characterization and engineering of a plastic-degrading aromatic polyesterase
作者: Austin H.P.; Allen M.D.; Donohoe B.S.; Rorrer N.A.; Kearns F.L.; Silveira R.L.; Pollard B.C.; Dominick G.; Duman R.; Omari K.E.; Mykhaylyk V.; Wagner A.; Michener W.E.; Amore A.; Skaf M.S.; Crowley M.F.; Thorne A.W.; Johnson C.W.; Lee Woodcock H.; McGeehan J.E.; Beckham G.T.
刊名: Proceedings of the National Academy of Sciences of the United States of America
ISSN: 0027-8424
出版年: 2018
卷: 115, 期:19
起始页码: E4350
结束页码: E4357
语种: 英语
英文关键词: Biodegradation ; Cutinase ; Plastics recycling ; Poly(ethylene furanoate) ; Poly(ethylene terephthalate)
Scopus关键词: cutinase ; esterase ; hydrolase ; PETase ; plastic ; polyester ; polyethylene 2,5 furandicarboxylate ; polyethylene terephthalate ; triacylglycerol lipase ; unclassified drug ; bacterial protein ; esterase ; polyethylene terephthalate ; Article ; bacterium ; biodegradation ; controlled study ; crystal structure ; depolymerization ; differential scanning calorimetry ; enzyme active site ; enzyme engineering ; enzyme substrate complex ; Ideonella sakaiensis ; molecular docking ; molecular dynamics ; nonhuman ; priority journal ; recycling ; scanning electron microscopy ; Burkholderiales ; chemistry ; enzyme specificity ; enzymology ; genetics ; protein engineering ; X ray crystallography ; Bacterial Proteins ; Burkholderiales ; Crystallography, X-Ray ; Esterases ; Polyethylene Terephthalates ; Protein Engineering ; Substrate Specificity
英文摘要: Poly(ethylene terephthalate) (PET) is one of the most abundantly produced synthetic polymers and is accumulating in the environment at a staggering rate as discarded packaging and textiles. The properties that make PET so useful also endow it with an alarming resistance to biodegradation, likely lasting centuries in the environment. Our collective reliance on PET and other plastics means that this buildup will continue unless solutions are found. Recently, a newly discovered bacterium, Ideonella sakaiensis 201-F6, was shown to exhibit the rare ability to grow on PET as a major carbon and energy source. Central to its PET biodegradation capability is a secreted PETase (PET-digesting enzyme). Here, we present a 0.92 Å resolution X-ray crystal structure of PETase, which reveals features common to both cutinases and lipases. PETase retains the ancestral α/β-hydrolase fold but exhibits a more open active-site cleft than homologous cutinases. By narrowing the binding cleft via mutation of two active-site residues to conserved amino acids in cutinases, we surprisingly observe improved PET degradation, suggesting that PETase is not fully optimized for crystalline PET degradation, despite presumably evolving in a PET-rich environment. Additionally, we show that PETase degrades another semiaromatic polyester, polyethylene-2,5-furandicarboxylate (PEF), which is an emerging, bioderived PET replacement with improved barrier properties. In contrast, PETase does not degrade aliphatic polyesters, suggesting that it is generally an aromatic polyesterase. These findings suggest that additional protein engineering to increase PETase performance is realistic and highlight the need for further developments of structure/activity relationships for biodegradation of synthetic polyesters. © 2018 National Academy of Sciences. All rights reserved.
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资源类型: 期刊论文
标识符: http://119.78.100.158/handle/2HF3EXSE/163719
Appears in Collections:气候变化与战略

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作者单位: Austin, H.P., Molecular Biophysics Laboratories, School of Biological Sciences, Institute of Biological and Biomedical Sciences, University of Portsmouth, Portsmouth, PO1 2DY, United Kingdom; Allen, M.D., Molecular Biophysics Laboratories, School of Biological Sciences, Institute of Biological and Biomedical Sciences, University of Portsmouth, Portsmouth, PO1 2DY, United Kingdom; Donohoe, B.S., Biosciences Center, National Renewable Energy Laboratory, Golden, CO 80401, United States; Rorrer, N.A., National Bioenergy Center, National Renewable Energy Laboratory, Golden, CO 80401, United States; Kearns, F.L., Department of Chemistry, University of South Florida, Tampa, FL 33620-5250, United States; Silveira, R.L., Biosciences Center, National Renewable Energy Laboratory, Golden, CO 80401, United States, Institute of Chemistry, University of Campinas, Campinas, Sao Paulo 13083-970, Brazil; Pollard, B.C., Department of Chemistry, University of South Florida, Tampa, FL 33620-5250, United States; Dominick, G., National Bioenergy Center, National Renewable Energy Laboratory, Golden, CO 80401, United States; Duman, R., Diamond Light Source, Harwell Science and Innovation Campus, Didcot, OX11 0DE, United Kingdom; Omari, K.E., Diamond Light Source, Harwell Science and Innovation Campus, Didcot, OX11 0DE, United Kingdom; Mykhaylyk, V., Diamond Light Source, Harwell Science and Innovation Campus, Didcot, OX11 0DE, United Kingdom; Wagner, A., Diamond Light Source, Harwell Science and Innovation Campus, Didcot, OX11 0DE, United Kingdom; Michener, W.E., National Bioenergy Center, National Renewable Energy Laboratory, Golden, CO 80401, United States; Amore, A., Biosciences Center, National Renewable Energy Laboratory, Golden, CO 80401, United States; Skaf, M.S., Institute of Chemistry, University of Campinas, Campinas, Sao Paulo 13083-970, Brazil; Crowley, M.F., Biosciences Center, National Renewable Energy Laboratory, Golden, CO 80401, United States; Thorne, A.W., Molecular Biophysics Laboratories, School of Biological Sciences, Institute of Biological and Biomedical Sciences, University of Portsmouth, Portsmouth, PO1 2DY, United Kingdom; Johnson, C.W., National Bioenergy Center, National Renewable Energy Laboratory, Golden, CO 80401, United States; Lee Woodcock, H., Department of Chemistry, University of South Florida, Tampa, FL 33620-5250, United States; McGeehan, J.E., Molecular Biophysics Laboratories, School of Biological Sciences, Institute of Biological and Biomedical Sciences, University of Portsmouth, Portsmouth, PO1 2DY, United Kingdom; Beckham, G.T., National Bioenergy Center, National Renewable Energy Laboratory, Golden, CO 80401, United States

Recommended Citation:
Austin H.P.,Allen M.D.,Donohoe B.S.,et al. Characterization and engineering of a plastic-degrading aromatic polyesterase[J]. Proceedings of the National Academy of Sciences of the United States of America,2018-01-01,115(19)
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