ArticleScientific reports2021
An absorbance method for analysis of enzymatic degradation kinetics of poly(ethylene terephthalate) films.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed.
- Isosteric Engineering of Enzymes: Overcoming Activity-Stability Trade-Offs by Site-Selective CH → N Substitutions.Angewandte Chemie (International ed. in English) · 2026Article
- Robust cellular transformations of PET deconstruction products by import of glycol esters.Science advances · 2026Article
- Dissolution-Precipitation Using Natural Terpenes as Pretreatment for PET Enzymatic Depolymerization.ACS omega · 2026Article
- Computer-guided enzyme engineering of PET hydrolase mutants towards improved PET affinity.BMC biotechnology · 2026Article
- Mechanistic insights into modulation of productive substrate accessibility for efficient PET depolymerization.Nature communications · 2026Article
- Systematic optimization and characterization of bacterial depolymerization of poly(ethylene terephthalate) plastics.Scientific reports · 2026Article
- Inactivation of PETase at Interfaces Inhibits PET Plastic Depolymerization.ACS sustainable chemistry & engineering · 2026Article
- Engineering a robust IsPETase for energy-efficient PET depolymerization in natural seawater at ambient temperatures.Advanced biotechnology · 2026Article
- EngineeringFrontiers in systems biology · 2026Article
- Disordered N-termini enhance the thermostability of SGNH-hydrolase family polyesterases.Protein science : a publication of the Protein Society · 2026Article
- Thermostable Bacterial Esterases From Lipase Family 1.5 Degrade Compostable Polyesters PBAT and PBSA.MicrobiologyOpen · 2025Article
- Construction of microbial systems for polyethylene terephthalate degradation.Synthetic and systems biotechnology · 2025Review
- The Esterase Gs Derived fromBiology · 2025Article
- Machine Learning-Guided Identification of PET Hydrolases from Natural Diversity.ACS catalysis · 2025Article
- Protocol for engineering poly(ethylene terephthalate) hydrolases via directed evolution using a high-throughput screening assay.STAR protocols · 2025Article
- Engineering PHL7 for improved poly(ethylene terephthalate) depolymerization via rational design and directed evolution.Chem catalysis · 2025Article
- Article
- Predicting protein stability changes upon mutations with dual-view ensemble learning from single sequence.Briefings in bioinformatics · 2025Article
- Standardization guidelines and future trends for PET hydrolase research.Nature communications · 2025Review
- Emerging Biochemical Conversion for Plastic Waste Management: A Review.Molecules (Basel, Switzerland) · 2025Review
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3 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Increased interest in poly(ethylene terephthalate) (PET)-degrading enzymes (PETases) have generated efforts to find mutants with improved catalytic activity and thermostability. Here, we present a simple and fast method to determine relative enzyme kinetics through bulk absorbance measurements of released products over time. A thermostable variant of PETase from Ideonella sakaiensis was engineered (R280A S121E D186H N233C S282C) with a denaturation temperature of 69.4 ± 0.3 °C. This was used to assess the method's ability to determine relative enzyme kinetics across variants and reveal structure-function relationships. Measurements at 24 and 72 h at 400 nM of enzyme suggest that the mutations improved catalytic rates 5- to 7-fold. On the contrary, kinetic analyses of the thermostable variant and wild-type reveal different reaction trajectories despite similar maximum catalytic rates, resulting in higher product accumulation from the thermostable variant over time. The results of the assay support the necessity for kinetic measurements to determine relationships between sequence and function for IsPETase and other PET hydrolases.
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