Ackermann YS, Li WJ, Op de Hipt L et al (2021) Engineering adipic acid metabolism in Pseudomonas putida. Metab Eng 67:29–40. https://doi.org/10.1016/j.ymben.2021.05.001
Akutsu-Shigeno Y, Adachi Y, Yamada C et al (2006) Isolation of a bacterium that degrades urethane compounds and characterization of its urethane hydrolase. Appl Microbiol Biotechnol 70:422–429. https://doi.org/10.1007/s00253-005-0071-1
Alariqi SAS, Pratheep Kumar A, Rao BSM, Singh RP (2006) Biodegradation of γ-sterilised biomedical polyolefins under composting and fungal culture environments. Polym Degrad Stab 91:1105–1116. https://doi.org/10.1016/j.polymdegradstab.2005.07.004
Almeida EL, Rincón AFC, Jackson SA, Dobson ADW (2019) In: Silico screening and heterologous expression of a polyethylene terephthalate hydrolase (PETase)-like enzyme (SM14est) with polycaprolactone (PCL)-degrading activity, from the marine sponge-derived strain Streptomyces sp. SM14 Front Microbiol 10:2187. https://doi.org/10.3389/fmicb.2019.02187
Alessandra P, Cinzia P, Paola G et al (2010) Heterologous laccase production and its role in industrial applications. Bioeng Bugs 1:252–262. https://doi.org/10.4161/bbug.1.4.11438
Al-Tammar KA, Omar O, Abdul Murad AM, Abu Bakar FD (2016) Expression and characterization of a cutinase (AnCUT2) from Aspergillus niger. Open Life Sci 11:29–38. https://doi.org/10.1515/biol-2016-0004
Amobonye A, Bhagwat P, Singh P, Pillai S (2021) Plastic biodegradation: frontline microbes and their enzymes. Sci Total Environ 759:143536. https://doi.org/10.1016/j.scitotenv.2020.143536
Andler R (2020) Bacterial and enzymatic degradation of poly(cis-1,4-isoprene) rubber: novel biotechnological applications. Biotechnol Adv 44:107606. https://doi.org/10.1016/j.biotechadv.2020.107606
Andler R, Hiessl S, Yücel O et al (2018) Cleavage of poly(cis-1,4-isoprene) rubber as solid substrate by cultures of Gordonia polyisoprenivorans. N Biotechnol 44:6–12. https://doi.org/10.1016/j.nbt.2018.03.002
Andler R, Valdés C, Díaz-Barrera A, Steinbüchel A (2020) Biotransformation of poly(cis-1,4-isoprene) in a multiphase enzymatic reactor for continuous extraction of oligo-isoprenoid molecules. N Biotechnol 58:10–16. https://doi.org/10.1016/j.nbt.2020.05.001
Andrić P, Meyer AS, Jensen PA, Dam-Johansen K (2010) Reactor design for minimizing product inhibition during enzymatic lignocellulose hydrolysis: I. significance and mechanism of cellobiose and glucose inhibition on cellulolytic enzymes. Biotechnol Adv 28:308324. https://doi.org/10.1016/j.biotechadv.2010.01.003
Arkatkar A, Arutchelvi J, Bhaduri S et al (2009) Degradation of unpretreated and thermally pretreated polypropylene by soil consortia. Int Biodeterior Biodegrad 63:106–111. https://doi.org/10.1016/j.ibiod.2008.06.005
Arpia AA, Chen WH, Ubando AT et al (2021) Microplastic degradation as a sustainable concurrent approach for producing biofuel and obliterating hazardous environmental effects: a state-of-the-art review. J Hazard Mater 418:126381. https://doi.org/10.1016/j.jhazmat.2021.126381
Austin HP, Allen MD, Donohoe BS et al (2018) Characterization and engineering of a plastic-degrading aromatic polyesterase. Proc Natl Acad Sci USA 115:4350–4357. https://doi.org/10.1073/pnas.1718804115
Auta HS, Emenike CU, Jayanthi B, Fauziah SH (2018) Growth kinetics and biodeterioration of polypropylene microplastics by Bacillus sp. and Rhodococcus sp. isolated from mangrove sediment. Mar Pollut Bull 127:15–21. https://doi.org/10.1016/j.marpolbul.2017.11.036
Barth M, Wei R, Oeser T et al (2015) Enzymatic hydrolysis of polyethylene terephthalate films in an ultrafiltration membrane reactor. J Memb Sci 494:182–187. https://doi.org/10.1016/j.memsci.2015.07.030
Bermúdez-García E, Peña-Montes C, Martins I et al (2019) Regulation of the cutinases expressed by Aspergillus nidulans and evaluation of their role in cutin degradation. Appl Microbiol Biotechnol 103:3863–3874. https://doi.org/10.1007/s00253-019-09712-3
Brueckner T, Eberl A, Heumann S et al (2008) Enzymatic and chemical hydrolysis of Poly(ethylene terephthalate) fabrics. J Polym Sci Part A Polym Chem 46:6435–6443. https://doi.org/10.1002/pola.22952
Carniel A, Valoni É, Nicomedes J et al (2017) Lipase from Candida antarctica (CALB) and cutinase from Humicola insolens act synergistically for PET hydrolysis to terephthalic acid. Process Biochem 59:84–90. https://doi.org/10.1016/j.procbio.2016.07.023
Chandra R, Chowdhary P (2015) Properties of bacterial laccases and their application in bioremediation of industrial wastes. Environ Sci Process Impacts 17:326–342. https://doi.org/10.1039/c4em00627e
Chen S, Su L, Chen J, Wu J (2013) Cutinase: characteristics, preparation, and application. Biotechnol Adv 31:1754–1767. https://doi.org/10.1016/j.biotechadv.2013.09.005
Chen CC, Han X, Ko TP et al (2018) Structural studies reveal the molecular mechanism of PETase. FEBS J 285:3717–3723. https://doi.org/10.1111/febs.14612
Chen CC, Dai L, Ma L, Guo RT (2020) Enzymatic degradation of plant biomass and synthetic polymers. Nat Rev Chem 4:114–116. https://doi.org/10.1038/s41570-020-0163-6
Cowan AR, Costanzo CM, Benham R et al (2022) Fungal bioremediation of polyethylene: Challenges and perspectives. J Appl Microbiol 132:78–89. https://doi.org/10.1111/jam.15203
Cui Y, Chen Y, Liu X et al (2021) Computational redesign of a PETase for plastic biodegradation under ambient condition by the GRAPE strategy. ACS Catal 11:1340–1350. https://doi.org/10.1021/acscatal.0c05126
Danso D, Schmeisser C, Chow J et al (2018) New insights into the function and global distribution of polyethylene terephthalate (PET)-degrading bacteria and enzymes in marine and terrestrial metagenomes. Appl Environ Microbiol 53:1689–1699. https://doi.org/10.1128/AEM.02773-17
Danso D, Chow J, Streit WR (2019) Plastics: environmental and biotechnological perspectives on microbial degradation. Appl Environ Microbiol 85:e01095-e1119. https://doi.org/10.1128/AEM.01095-19
Deguchi T, Kitaoka Y, Kakezawa M, Nishida T (1998) Purification and characterization of a nylon-degrading enzyme. Appl Environ Microbiol 64:1366–1371. https://doi.org/10.1128/aem.64.4.1366-1371.1998
do Canto VP, Thompson CE, Netz PA (2019) Polyurethanases: Three-dimensional structures and molecular dynamics simulations of enzymes that degrade polyurethane. J Mol Graph Model 89:82–95. https://doi.org/10.1016/j.jmgm.2019.03.001
Du J, Zhang F, Li Y et al (2014) Enzymatic liquefaction and saccharification of pretreated corn stover at high-solids concentrations in a horizontal rotating bioreactor. Bioprocess Biosyst Eng 37:173–181. https://doi.org/10.1007/s00449-013-0983-6
Ece S, Lambertz C, Fischer R, Commandeur U (2017) Heterologous expression of a Streptomyces cyaneus laccase for biomass modification applications. AMB Express 7:86. https://doi.org/10.1186/s13568-017-0387-0
Eibes G, López C, Moreira MT et al (2007) Strategies for the design and operation of enzymatic reactors for the degradation of highly and poorly soluble recalcitrant compounds. Biocatal Biotransform 25:260–268. https://doi.org/10.1080/10242420701444371
Ellis LD, Rorrer NA, Sullivan KP et al (2021) Chemical and biological catalysis for plastics recycling and upcycling. Nat Catal 4:539–556. https://doi.org/10.1038/s41929-021-00648-4
Falkenstein P, Gräsing D, Bielytskyi P et al (2020) UV pretreatment impairs the enzymatic degradation of polyethylene terephthalate. Front Microbiol 11:689. https://doi.org/10.3389/fmicb.2020.00689
Fei X, Fei X, Fei X et al (2020) Biobased poly(ethylene 2,5-furancoate): no longer an alternative, but an irreplaceable polyester in the polymer industry. ACS Sustain Chem Eng 8:8471–8485. https://doi.org/10.1021/acssuschemeng.0c01862
Ferreira RDG, Azzoni AR, Freitas S (2018) Techno-economic analysis of the industrial production of a low-cost enzyme using E. coli: the case of recombinant β-glucosidase. Biotechnol Biofuels 11:81. https://doi.org/10.1186/s13068-018-1077-0
Fincher EL, Payne WJ (1962) Bacterial utilization of ether glycols. Appl Microbiol 10:542–547. https://doi.org/10.1128/aem.10.6.542-547.1962
Frank R, Krinke D, Sonnendecker C et al (2022) Real-time noninvasive analysis of biocatalytic PET degradation. ACS Catal 12:25–35. https://doi.org/10.1021/acscatal.1c03963
Fujisawa M, Hirai H, Nishida T (2001) Degradation of polyethylene and nylon-66 by the laccase-mediator system. J Polym Environ 103–108. https://doi.org/10.1023/A:1020472426516
Gamerith C, Vastano M, Ghorbanpour SM et al (2017) Enzymatic degradation of aromatic and aliphatic polyesters by P. pastoris expressed cutinase 1 from Thermobifida cellulosilytica. Front Microbiol 8:938. https://doi.org/10.3389/fmicb.2017.00938
García-Aguirre M, Sáenz-Álvaro VA, Rodríguez-Soto MA et al (2009) Strategy for biotechnological process design applied to the enzymatic hydrolysis of agave fructo-oligosaccharides to obtain fructose-rich syrups. J Agric Food Chem 57:10205–10210. https://doi.org/10.1021/jf902855q
Gaston LW, Stadtman ER (1963) Fermentation of ethylene glycol by Clostridium glycolicum, sp. n. J Bacteriol 85:356–362. https://doi.org/10.1128/jb.85.2.356-362.1963
Gewert B, Plassmann MM, Macleod M (2015) Pathways for degradation of plastic polymers floating in the marine environment. Environ Sci Process Impacts 17:1513–1521. https://doi.org/10.1039/C5EM00207A
Gomes DS, Matamá T, Cavaco-Paulo A et al (2013) Production of heterologous cutinases by E. coli and improved enzyme formulation for application on plastic degradation. Electron J Biotechnol 16:1–14. https://doi.org/10.2225/vol16issue5-fulltext-12
Gricajeva A, Nadda AK, Gudiukaite R (2022) Insights into polyester plastic biodegradationby carboxyl ester hydrolases. J Chem Technol Biotechnol 97:359–380. https://doi.org/10.1002/jctb.6745
Guadix-Montero S, Sankar M (2018) Review on catalytic cleavage of C-C inter-unit linkages in lignin model compounds: towards lignin depolymerisation. Top Catal 61:183–198. https://doi.org/10.1007/s11244-018-0909-2
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