Identification of prospective PETases across prokaryotes using an in silico approach

Of these eight, three PETases from Halopseudomonas pertucinogena, Halopseudomonas bauzanensis and Ketobacter sp. revealed significant similarity in structure and conformational stability to the PETase from I. sakaiensis, as was evident from the analysis of their molecular dynamics parameters. Principal Component Analysis and the free energy landscape during binding to BHET also validated the hypothesis, and these three PETases could be immediately explored for possible plastic degradation activity.