ArticleACS sustainable chemistry & engineering2025
Functional and Structural Characterization of PETase SM14 from Marine-Sponge Streptomyces sp. Active on Polyethylene Terephthalate.
Article in ACS sustainable chemistry & engineering, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Lignocellulose-mediated selection of potential halophilic PET-degrading enzymes from mangrove soil.Nature communications · 2026Article
- Temperature-Dependent Active-Site Rearrangements of PETaseSM14: Insights from Molecular Dynamics Simulations.International journal of molecular sciences · 2026Article
- Identification and characterization of R75estA, a halophilic polyester-degrading enzyme from a marine bacterium.Frontiers in microbiology · 2026Article
- The effect of ionic strength on PETase enzymes: An experimental and computational study.Protein science : a publication of the Protein Society · 2026Article
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The recent discovery of the PETase enzyme family offers a sustainable solution for depolymerizing poly-(ethylene terephthalate) (PET), one of the most widespread plastic compounds, under mild conditions. This enables the environmentally beneficial conversion of plastic waste into value-added products. Among this enzyme family, PETase from Ideonella sakaiensis has been the most extensively studied. Although other similar enzymes have been discovered, our knowledge about the catalytic and structural properties of this class remains limited. In this study, a PETase-like enzyme (PETase SM14) from Streptomyces sp. SM14 was heterologously produced in Escherichia coli, and its activity was tested on post-consumer plastic substrates using high-performance liquid chromatography for product quantification as well as scanning electron microscopy and atomic force microscopy for substrate surface imaging evaluation. PETase SM14 exhibited high salt tolerance (1.5 M), good heat resistance (Tm 56.26 °C), and optimal activity at pH 9.0, highlighting its potential for PET waste bioremediation. Furthermore, its X-ray crystal structure was solved at 1.43 Å resolution, revealing conserved features of the PETase family with potential relevance for future engineering applications.
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