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Related Concept Videos

Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.
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Bioremediation is an environmentally sustainable process that employs living organisms—primarily microorganisms—to degrade or neutralize pollutants from contaminated environments. In oil spills and hydrocarbon pollution, bioremediation involves the use of hydrocarbon-degrading bacteria to transform toxic compounds into less harmful substances. This approach leverages natural microbial metabolic processes and is considered both cost-effective and ecologically favorable compared to physical or...
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Strain improvement is a foundational strategy in industrial microbiology aimed at maximizing microbial productivity, particularly because natural isolates typically yield commercially valuable products in very low concentrations. Although optimizing the culture medium and environmental conditions can improve yields, these adjustments are inherently limited by the organism’s genetic potential. As a result, the focus shifts toward genetic modifications to enhance biosynthetic capacity. The...
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Polyethylene terephthalate (PET) is a synthetic polymer widely utilized in the packaging industry, particularly for bottles and containers. Due to its chemical stability and durability, PET accumulates in the environment, contributing significantly to plastic pollution. It comprises repeating units of terephthalic acid and ethylene glycol, resulting in a semi-crystalline structure that is resistant to natural degradation processes.A notable breakthrough in plastic biodegradation came with the...
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Updated: Jul 1, 2026

A Toolkit to Enable Hydrocarbon Conversion in Aqueous Environments
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Computer-guided enzyme engineering of PET hydrolase mutants towards improved PET affinity.

Alexandra Balola1, Sofia Ferreira2, Caio Silva Souza1

  • 1Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Oeiras, Portugal.

BMC Biotechnology
|June 29, 2026
PubMed
Summary

Targeted active-site engineering using the GDEE platform significantly boosted PETase enzyme efficiency for plastic degradation. A key S238Y mutation enhanced performance by up to 3.4-fold, offering a sustainable solution for plastic waste.

Keywords:
Catalytic efficiencyEnzyme engineeringMolecular dynamicsPETasePlastic degradationPolyethylene terephthalateSubstrate binding affinity

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Area of Science:

  • Biotechnology and Environmental Science
  • Enzyme Engineering
  • Protein Engineering

Background:

  • Polyethylene Terephthalate (PET) pollution is a significant environmental concern.
  • Enzymatic degradation using PETase offers a sustainable solution for PET recycling.
  • Existing research often focuses on thermal stability, neglecting active-site engineering for catalytic efficiency.

Purpose of the Study:

  • To explore active-site mutations for enhancing PETase catalytic efficiency.
  • To utilize an in silico platform for high-throughput enzyme engineering.
  • To identify specific mutations that improve PET degradation performance.

Main Methods:

  • Employed the Gene Discovery and Enzyme Engineering (GDEE) platform for in silico protein engineering.
  • Generated and screened thousands of PETase variants with a focus on active-site mutations.
  • Evaluated variants using docking studies and ranked them based on binding affinity and catalytic geometry.
  • Introduced the identified S238Y mutation into FAST-PETase (FP) and ThermoStable-PETase (TSP) scaffolds.

Main Results:

  • Identified the S238Y mutation as a key enhancer of PET degradation.
  • Achieved a 2.2-fold increase in degradation for FP and a 3.4-fold increase for TSP.
  • FP S238Y showed a 14.8-fold increase in bulk activity, TSP S238Y a 25.8-fold increase.
  • Observed enhanced catalytic efficiency and reduced enzyme inhibition with the S238Y mutation.

Conclusions:

  • Targeted active-site engineering is a powerful strategy for developing efficient biocatalysts.
  • The GDEE platform accelerates the discovery of improved enzymes for plastic waste remediation.
  • The S238Y mutation represents a significant advancement in PETase-based plastic degradation.