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Heterologous expression and characterization of Rhodococcus opacus R7 laccase-like multicopper oxidase (LMCO1) enzyme
Mahboobeh Pishan1, Sima Sazegari2, Ali Niazi3
1Department of Food Science and Technology, Shiraz University, Shiraz, Fars, Iran.
Scientific Reports
|June 26, 2026
Summary
This study shows laccase-like multicopper oxidase (LMCO1) can efficiently degrade polyethylene (PE) plastics. Machine learning and enzyme expression confirm LMCO1 as a promising, eco-friendly catalyst for plastic waste reduction.
Area of Science:
- Biotechnology
- Environmental Science
- Materials Science
Background:
- Polyethylene (PE) production is rising, causing environmental concerns.
- Effective strategies are needed to degrade PE and mitigate its environmental impact.
Purpose of the Study:
- To investigate the potential of laccase-like multicopper oxidase (LMCO1) in the oxidative degradation of PE.
- To evaluate LMCO1's efficiency using machine learning, recombinant expression, and physio-chemical analyses.
Main Methods:
- Machine learning analysis of RNA-seq data to identify LMCO1's role in PE degradation.
- Recombinant expression and characterization of LMCO1 activity.
- Physio-chemical assays including weight loss, water contact angle, FTIR, and SEM to assess PE degradation.
Main Results:
- Cu²⁺ significantly enhanced LMCO1 activity by 490% at optimal pH 8 and 60°C.
- LMCO1 achieved a 14.28% weight loss rate in LDPE over 72 hours, reducing water contact angle.
- FTIR and SEM confirmed surface modification and structural damage, indicating effective PE degradation.
Conclusions:
- LMCO1 demonstrates high potential for efficient oxidative degradation of PE films and particles without pre-treatment.
- LMCO1 is presented as a promising, environmentally friendly catalyst for plastic degradation, validated by machine learning and experimental data.
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