Enzymatic degradation of double bonds

One of the pressing environmental problems of our time is non-degradable waste, a large part of which comes from electronics. As time goes on, the problem is becoming even more challenging. However, some believe that conjugated polymers can help to combat this by opening up the possibility of creating biodegradable products, in particular in electronics. In a 2018 study, myeloperoxidase (MPO) was found to be able to cleave semiconducting polymer nanoparticles that have a similar molecular structure to conjugated polymers used for device applications. To this date that is the only known available study on the topic, which makes for large knowledge gaps. The aim of this study was to investigate enzymes capable of catalyzing the cleavage of alkenes to find possible candidates for further research on the enzymatic cleavage of conjugated polymers. The project was divided into two parts: a literature study and laboratory work. The literature study was based on previous research and focused on alkene-cleaving enzymes in compost. The following key factors were used to determine their suitability: substrate, subcellular location, optimal pH and temperature, and abundance in compost. As for the laboratory part of the project, the goal was to assess the stability and catalytic activity of MPO using an activity assay kit. At first, a few different enzymes were considered as possible candidates but after further investigation, some were deemed to be more suitable than others. It was concluded that horseradish peroxidase, laccase, and sectrome of Pseudomonas putida had the greatest potential to degrade alkenes in compost. However, each one possesses its own set of benefits and drawbacks. As for the laboratory part of this project, due to a manufacturing error of one of the reagents in the activity assay kit used, neither the activity nor the stability of MPO could be determined.