Role of conserved regions in PETase-mediated degradation

Abstract

Plastic pollution generated by polyethylene terephthalate (PET) is a major environmental issue due to its high stability and resistance to natural degradation. In recent years, several bacterial genus like Ideonella , Pseudomonas , Bacillus , Thermobifida , and Rhodococcus , have been reported for their ability to break down PET. An enzyme PETase has been identified in Ideonella sakaiensis which shows an important role in catalytic activity in PET degradation. It also found that PETase enzyme has a conserved region which contains catalytic amino acid triad (-SHD-) for substrate binding and enzyme stability. Previous studies have also reported the PET-degrading potential of R. pyridinivorans ; however, the molecular characteristics of its PET esterase-like proteins remain poorly understood. Therefore, to decipher the molecular details a biodegradation, a bioinformatic approach was utilized. In this study, we identified the potential PET-degrading enzymes using in silico approach. Previous studies have reported that the Abhydrolase_3 (PF07859) domain is associated with PET esterase-like proteins in R. pyridinivorans . Bioinformatic analysis revealed PET esterase-like proteins in R. pyridinivorans which contain Abhydrolase_3 domain having PETase like activity. Alpha-fold was utilized for creation of three-dimensional structure of PETase for R. pyridinivorans . Present study reveals the presence of PETase-like proteins in R. pyridinivorans , which was also confirmed at motif level evidence. The results may pave a direction in confirming the biodegradation potential of R. pyridinivorans.