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Related Concept Videos

Proofreading01:31

Proofreading

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Synthesis of new DNA molecules is carried out by the enzyme DNA polymerase, which adds nucleotides on the daughter strand complementary to the template DNA strand. DNA polymerase has a higher affinity to add the correct base and ensures fidelity during DNA replication. Furthermore,  it exhibits proofreading activity during replication, using an exonuclease domain that cuts off incorrect nucleotides from the nascent DNA strand.
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Because the DNA segments are cut and reorganized in a direction-specific manner, site-specific recombination has emerged as an efficient genetic engineering technique. Flippase and Cyclization recombinases or Flp and Cre, respectively, are two members of the tyrosine recombinase family derived from bacteriophages, that are used to mediate site-specific DNA insertions, deletions, and targeted expression of proteins in mammalian cell lines.
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Step-growth or condensation polymerization is a stepwise reaction of bi or multifunctional monomers to form long-chain polymers. As all the monomers are reactive, most of the monomers are consumed at the early stages of the reaction to form small chains of reactive oligomers, which then combine to form long polymer chains in the late stages. Hence, the reaction has to proceed for a long time to achieve high molecular weight polymers.
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Directed Evolution of an Efficient Polycarbonate Depolymerase With Exceptional Operational Stability.

Henry A Jones1, Amy E Hutton1,2, Dominic Harris-Jukes3

  • 1Manchester Institute of Biotechnology, School of Chemistry, The University of Manchester, Manchester, UK.

Angewandte Chemie (International Ed. in English)
|March 23, 2026
PubMed
Summary

Researchers engineered plastic-degrading enzymes to recycle polycarbonate, a valuable polymer. This directed evolution platform rapidly breaks down polycarbonate into its basic components for efficient recycling.

Keywords:
biocatalysisdepolymerizationdirected evolutionpolycarbonatepolymer hydrolase

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Area of Science:

  • Biotechnology
  • Polymer Science
  • Enzyme Engineering

Background:

  • A high-throughput directed evolution platform was previously developed for engineering polymer-degrading enzymes.
  • This platform was successfully used to create HotPETase, an efficient and thermostable variant of IsPETase.

Purpose of the Study:

  • To demonstrate the utility of the directed evolution platform for re-engineering PET-degrading enzymes to recycle other aromatic-containing commodity polymers.
  • To engineer a promiscuous poly(bisphenol-A carbonate) (PC) depolymerase activity of LCCICCG into an efficient polycarbonate hydrolase.

Main Methods:

  • Directed evolution was employed to enhance the poly(bisphenol-A carbonate) (PC) depolymerase activity of LCCICCG.
  • The engineered enzyme was evaluated for improved solvent tolerance, operational stability at elevated temperatures, and alleviation of enzyme-concentration dependent inhibition.

Main Results:

  • An engineered polycarbonate hydrolase, termed PC-2, was developed with enhanced activity and stability.
  • PC-2 demonstrated improved solvent tolerance and operational stability at elevated temperatures.
  • Enzyme-concentration dependent inhibition observed in the parent enzyme was alleviated in PC-2.
  • PC-2 achieved rapid and complete depolymerization of a PC film to bisphenol-A (BPA) within 6 hours at 75°C.

Conclusions:

  • The directed evolution platform is effective for adapting plastic-degrading enzymes to new polymer classes.
  • Engineered enzymes can be readily developed for the efficient recycling of valuable commodity polymers like polycarbonate.
  • This approach holds promise for advancing sustainable plastic recycling technologies.