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Enzymatic degradation of phthalate esters in the environment: Advances, challenges and opportunities
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Fibre- and Polymer Technology. KTH, Centres, Science for Life Laboratory, SciLifeLab.ORCID iD: 0000-0002-2757-9273
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Fibre- and Polymer Technology. KTH, Centres, Science for Life Laboratory, SciLifeLab.ORCID iD: 0000-0002-4066-2776
2025 (English)In: Chemical Engineering Journal, ISSN 1385-8947, E-ISSN 1873-3212, Vol. 508, article id 160640Article, review/survey (Refereed) Published
Abstract [en]

The continued growth in phthalate esters (PAEs) production (∼8 million tons per year) has led to the increased emissions of PAEs into atmospheric, soil, and aquatic environments, posing a serious threat to human and animal health. Microbial enzyme-mediated degradation is an effective remediation strategy for removing PAE contaminants in the environment. Several hydrolases from both culturable and non-culturable microorganisms have been identified with outstanding degradation capacities against PAEs. A hydrolase identified from Glutamicibacter sp. strain 0426 could completely degrade 300 mg/L of dibutyl phthalate (DBP) within 12 h at 32℃ and pH 6.9, and an esterase which was screened from a metagenomic library exhibited high hydrolytic activity (128 U/mg) toward DBP at 40℃ and pH 7.5. However, there are still only a limited number of PAE-degrading enzymes that have been fully characterized so far. Herein, we show the significant influence of PAEs on plastic recycling and environmental pollution. We review recent advances in the identification and isolation of PAE-degrading enzymes from diverse environments. We highlight the potential of metagenomic analyses for exploring novel and powerful PAE hydrolases. Moreover, we discuss a possible enzyme-catalyzed reaction mechanism for PAE hydrolysis given the scarce experimental evidence. The substrate specificity among different monoalkyl/dialkyl PAE hydrolases is attributed to the steric hindrance and electrostatic repulsion affecting the PAE binding to an enzyme. Furthermore, we discuss different directed evolution strategies for improving the performance of PAE-degrading enzymes. Several challenges and future directions in research on PAE-degrading enzymes are also identified.

Place, publisher, year, edition, pages
Elsevier BV , 2025. Vol. 508, article id 160640
Keywords [en]
Directed evolution, Enzymatic degradation, Metagenomics, Phthalate esters, Reaction mechanism
National Category
Molecular Biology Environmental Sciences Microbiology
Identifiers
URN: urn:nbn:se:kth:diva-361144DOI: 10.1016/j.cej.2025.160640ISI: 001437316100001Scopus ID: 2-s2.0-85218876132OAI: oai:DiVA.org:kth-361144DiVA, id: diva2:1944098
Note

QC 20250317

Available from: 2025-03-12 Created: 2025-03-12 Last updated: 2025-03-17Bibliographically approved

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Sun, ShengweiSyrén, Per-Olof

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