The new enzyme offers hope for reducing plastic pollution
DLP Report
PESHAWAR
A research team from Hubei University has made a significant breakthrough in plastic degradation by identifying a highly efficient enzyme capable of breaking down poly(butylene adipate-co-terephthalate) (PBAT), a widely used biodegradable plastic.
The enzyme, cutinase from Thermobifida fusca (TfCut), was found to degrade PBAT mulch films into small fragments and eventually dissolve them completely within two days.
The study revealed that the degradation process produces three intermediate compounds—BTa, ABTa, and TaBTa—before ending with terephthalic acid (TPA), which can be easily recycled. Researchers also engineered a more efficient version of the enzyme, TfCut-DM, which degrades PBAT even faster, leaving only TPA as the final product after 48 hours.
When the team engineered the enzyme by replacing a histidine-phenylalanine residue pair with serine-isoleucine, creating TfCut-DM, they observed an even more efficient degradation process.
In this case, only TPA remained, making the recycling of PBAT more straightforward.
Structural analysis showed that the engineered TfCut-DM has a flatter active site, allowing it to better bind and break down the plastic.
This discovery offers a promising solution for addressing plastic waste, especially in agricultural and packaging industries, and could pave the way for more sustainable recycling practices.
Moreover, the research findings and discovery holds potential for improving the management and recycling of PBAT, providing a more eco-friendly solution to plastic waste.
