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Discovery of a polyethylene biodegradable laccase from Acinetobacter dijkshoorniae

Informatica 2025 3 citations ? Citation count from OpenAlex, updated daily. May differ slightly from the publisher's own count.
Luxuan Wu, Xiufeng Wang, Anni Li, Haiyang Cui, Xiujuan Li

Summary

Researchers identified a novel laccase enzyme from Acinetobacter bacteria that is capable of breaking down polyethylene, one of the most widely used and persistent plastics. The enzyme demonstrates measurable biodegradation activity under laboratory conditions, offering a potential biological pathway for plastic waste remediation. This discovery adds to a growing toolkit of microbial enzymes being explored for enzymatic plastic recycling.

Polymers

Abstract Plastic waste management, especially polyethylene (PE), is a global challenge due to its chemical inertness and resistance to degradation. Herein, we isolated a bacterial strain, Acinetobacter dijkshoorniae PE‐9, which can degrade PE films. Over 40 days, the strain reduced the film weight by 5.1%, with degradation confirmed by SEM, FTIR, water contact angle (WCA), and GPC analysis. Using whole‐genome sequencing, transcriptomics, and sequence similarity network analysis, we identified the key degradation enzyme, a multicopper oxidase (AcMCO). The crude AcMCO reduced the WCA of PE films from 97.0° to 60.1%, with its effect supported by SEM and GC–MS analysis. Molecular dynamics simulations revealed the AcMCO‐PE interaction pattern, identifying a methionine‐rich region (AcMCO‐MetRich, residues 328–446) crucial for binding to the PE surface. These findings provide insights into microbial PE degradation and the potential of AcMCO in enhancing plastic recycling.

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