The durability of polyethylene terephthalate (PET) debris is a long-term environmental burden, and the recycling efforts used at the present lack sustainability. The recently discovered bacterial enzymes PETase and MHETase of Ideonella sakaiensis which specifically degrade PET represent a promising solution. They allow I. sakaiensis to use PET as its major energy and carbon source for growth and MHETase likely acts synergistically with PETase to depolymerize PET. In this protocol, the effect on the thermal stability of the enzyme MHETase by different ligands is analyzed.

thermal unfolding | enzyme stability | ligand-induced thermal stabilization | PR-P-012