Targeting microplastic particles in the void of diluted suspensions

Highlights

• Material binding peptides such as anchor peptides strongly bind synthetic polymers.

• The anchor peptide Tachystatin A2 served as adhesion promoter for cutinase Tcur1278.

• Tachystatin A2 enhanced enzymatic degradation of polyester-polyurethane by 6.6-fold.

• Tachystatin A2 reduced half-life of polyester-polyurethane nanoparticles by 6.7-fold.

• Prominent anchoring effect of adhesion promoter in highly diluted nanoparticles.

Abstract

Accumulation of microplastic in the environment and food chain will be a grand challenge for our society. Polyurethanes are widely used synthetic polymers in medical (e.g. catheters) and industrial products (especially as foams). Polyurethane is not abundant in nature and only a few microbial strains (fungi and bacteria) and enzymes (polyurethaneases and cutinases) have been reported to efficiently degrade polyurethane. Notably, in nature a long period of time (from 50 to >100 years depending on the literature) is required for degradation of plastics. Material binding peptides (e.g. anchor peptides) bind strongly to polymers such as polypropylene, polyethylene terephthalate, and polyurethane and can target specifically polymers. In this study we report the fusion of the anchor peptide Tachystatin A2 to the bacterial cutinase Tcur1278 which accelerated the degradation of polyester-polyurethane nanoparticles by a factor of 6.6 in comparison to wild-type Tcur1278. Additionally, degradation half-lives of polyester-polyurethane nanoparticles were reduced from 41.8 h to 6.2 h (6.7-fold) in a diluted polyester-polyurethane suspension (0.04% w/v).