CHARACTERIZATION OF PET HYDROLASES ASSOCIATED WITH MICROPLASTIC DEGRADING BACTERIA: AN IN-SILICO ANALYSIS

Abstract

Development of PETase variants with efficient potential of polyethylene terephthalate (PET) degradation is a sustainable route to microplastic (MP) bioremediation. Current study was initiated to explore the characteristics of PETases which could be helpful in enzyme modification via genetic engineering. For this purpose, three isoforms of enzyme associated with three different bacteria Piscinibacter sakaiensis,   Streptomyces labedae and Compostimonas suwonensis were selected. Amino acid sequence was retrieved from UNIPROT database and subjected to analysis via SOPMA tool, SWISS-MODEL server and MEME suite. The alpha helix, extended sheet and random coil observed were ranged between 78-113, 41-204 and 149-729, respectively. Monomeric three-dimensional (3D) configuration was observed in A0A0K8P6T7 and A0A2M9BCQ1 and dimeric configuration in A0ABP6QVC8. Conserved motifs (n = 11) were predicted for each of the three isoforms of PETases. These conserved domains might be targeted for engineering in order to enhance their binding affinity for PET. Considering the properties of PETases unraveled in current project and implementation of rational protein engineering alongwith in-silico strategies, might be helpful for the development of PETase super enzymes.

Keywords

PETases, polyethylene terephthalate, Ideonella sakaiensis, degradation, conserved motifs.