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From degradation to alleviation: Trichoderma facilitates plants resisting the PBAT stress through secreting a cutinase-like enzyme.
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Researchers found that overexpressing a cutinase-like enzyme (CUT2) in Trichoderma significantly accelerated PBAT biodegradable plastic depolymerization, reshaped rhizosphere microbial communities to activate aromatic degradation pathways, and reduced accumulation of phytotoxic monomers that inhibit plant growth — providing a fungal enzymatic strategy for managing biodegradable plastic toxicity in soil.
The ecological impacts of biodegradable plastics like poly (butylene adipate-co-terephthalate) (PBAT) demand urgent investigation due to their unresolved risks to soil-plant systems, including physical interference with root development, disruption of indigenous microbial ecology. While PBAT depolymerization is a prerequisite for its removal, the slow and inefficient breakdown of these polymers in soil often results in the persistent accumulation of phytotoxic monomers, creating a bottleneck for biological remediation. In this study, through transcriptomic and phylogenetic analyses, we identified a key secreted hydrolase CUT2, belonging to a distinct clade of cutinase-like polyester hydrolases. Overexpression of cut2 (OEThcut2) significantly enhanced PBAT depolymerization, resulting in 27.0% and 22.4% increases in the release of terephthalic acid (TPA) and butanediolic acid (BTA) compared to the wild-type strain, respectively. The direct catalytic activity of purified CUT2 was confirmed through vitro film weight-loss assays with a degradation rate of 4.3% observed. In pot experiments, integrated multi-omics analysis revealed that the OEThcut2 strain reconfigured the rhizosphere microbial community and activated the aromatic degradation pathways, coinciding with the attenuated accumulation of degradation monomers. Furthermore, the enrichment of carbohydrate-active enzymes (CAZys) and the reduction of monomer burdens which revitalized the tricarboxylic acid cycle (TCA) and normalized redox homeostasis thereby clearing the metabolic bottleneck for intermediate turnover. Complementary monomer-exposure assays established that the reduction of PBAT monomers is critical for alleviating plant oxidative stress and growth inhibition. These findings provide a depolymerization to detoxification framework that links fungal enzymatic activity to rhizosphere metabolic recovery, offering a robust strategy for mitigating biodegradable plastic toxicity in agroecosystem.
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Researchers found that the soil fungus Trichoderma can partially break down PBAT, a popular biodegradable plastic, by detecting the breakdown product terephthalic acid after exposure. However, the presence of microplastics reduced the fungus's ability to degrade common agricultural pesticides. This suggests that microplastic contamination in soil could interfere with natural pollution cleanup processes carried out by beneficial soil microorganisms.
Enzymatic biodegradation of poly(butylene adipate-co-terephthalate) (PBAT) microplastic by Trichoderma harzianum KKP534
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Scientists found that a common fungus called Trichoderma harzianum can break down PBAT, a "biodegradable" plastic often used in bags and packaging, by growing on it and releasing enzymes that create cracks and eat away at its surface. This matters because it shows a natural, low-cost way to help clear biodegradable plastics from the environment faster—potentially reducing the microplastic pollution that ends up in our soil, water, and eventually our food and bodies.
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Researchers found that the biocontrol fungus Trichoderma harzianum T4 alleviates stress caused by aged PBAT biodegradable microplastics in Nicotiana benthamiana plants, as demonstrated through physiological and multi-omics analyses. The fungus modulated plant metabolic and transcriptomic responses, suggesting a promising biological approach to mitigating biodegradable microplastic impacts in agricultural systems.
Hydrolytic Degradation of Polyethylene Terephthalate by Cutinase Enzyme Derived from Fungal Biomass–Molecular Characterization
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Researchers isolated cutinase and lipase enzymes from Aspergillus tamarii and Penicillium crustosum fungi and demonstrated their ability to catalyze hydrolytic degradation of PET plastic, offering a potential biological route for plastic waste breakdown.
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Scientists discovered that a marine fungus, Alternaria alternata, and two of its cutinase enzymes can break down PBAT — a biodegradable plastic used in packaging and mulch films — at body temperature (37°C), unlike most known plastic-degrading enzymes that require high heat. One of the enzymes completely degraded PBAT film within 48 hours, and engineering it slightly boosted recovery of the valuable terephthalic acid monomer to 96%. This is a significant advance for low-energy enzymatic plastic recycling and could help address the accumulation of PBAT microplastics in soil and marine environments.
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