Too much plastic is ending up in the ocean and making its way back onto our dinner plates. injures & kills marine life, spreads toxins & is a health threat. There are generally 3 p used for PET plastic recycling.
Alain Marty, the chief scientific officer at Carbios, teamed up with Isabelle Andre, an enzyme engineering expert at the University of Toulouse. They generated hundreds of mutant enzymes by changing amino acids in its crystalline structure at the binding site to make them more efficient. They also added in heat-stabilizing amino acids to make it able to withstand higher temperatures for longer. After testing all of them to find the most efficient PET breakers, they found the one best mutant enzyme. It’s 10,000 times more effective at PET bond-breaking than the native LCC. It can also work in temperatures at 72°C (which is around the temperature at which PET becomes molten) without breaking down. The research has been published in Nature.
Biodegrading PET takes two process, adsorption and degradation. The fusion protein was made to enhance the efficiency of adsorption, since the surface of PET film is hydrophobic and the surface of mLCC is hydrophilic. Constructing a mLCC-hydrophobin fusion protein will enhance the efficiency due to the unique properties of amphiphilicity and self-assembly of hydrophobins.
The second approach we used is Bacillus subtilis surface display. By combining mLCC with the anchor protein which forms the fusion protein, mLCC can be immobilized on the Bacillus subtilis cell surface to obtain a recyclable whole-cell biocatalyst, which can reduce costs and make mLCC more efficient at degrading PET.
