It has been reported that PET hydrolases can degrade PET into four products: terephthalic acid (TPA), ethylene glycol (EG), mono(2-hydroxyethyl) terephthalate (MHET), and bis(2-hydroxyethyl) terephthalate (BHET). SUPERB identified two highly efficient enzymes, IsPETase^PA and FAST-PETase-212/277, through literature research and utilized machine learning to predict mutation sites for improving enzyme activity or thermal stability.

To further enhance the industrial application of the enzyme and address environmental challenges, SUPERB combined the machine-learning-predicted mutation sites with glycosylation engineering. Subsequent wet lab experiments and molecular docking will be performed to validate the results, ultimately obtaining the optimal mutant enzyme.

SUPERB uses Pichia pastoris as the chassis cell to express enzymes. By optimizing promoters, signal peptides, and gene copy numbers, SUPERB has constructed Pichia pastoris strains with higher expression levels.

Since Komagataeibacter xylinus can convert and degrade ethylene glycol (EG) and terephthalic acid (TPA) into bacterial cellulose (BC), SUPERB exploits mixed fermentation with Pichia pastoris and Komagataeibacter xylinus. The composition of the culture medium and fermentation conditions are also optimized to achieve both plastic degradation and recycling.