Development of a framework towards the analysis of the enzymatic degradation of post-consumer polyethylene terephthalate using a photo-modulated PETase

In 2016 Yoshida, et al. discovered the enzyme PETase which has the highest natural activity on PET. To date, several studies about its structure, mechanism of action and enzyme kinetics have been carried out to elucidate the whole series of reactions that involve its catalytic performance. Furthermore, different research groups have tried to modify its stability, catalytic activity, and binding intending to condition the enzyme for scaling up and industrial application. Even though the modifications have been achieved positive results regarding the performance of the wild-type PETase, one of the biggest problems in the enzymatic hydrolysis of PET remains in the low bioavailability of the polymer to be attached in the binding site. To expand the comprehension of the binding process of PETase, the present work comprises the development of a framework for further modulation of PETase architecture using photo-switch based on azobenzene conjugated by thiol-ene click reaction as a novel strategy to reveal key dynamic regions in the binding process of the enzyme. Current results from molecular simulations support the application of a hinge-like structure to enlarge the cavity and enhance contact between the enzyme and the substrate, also a non-specific binding site unreported is defined and related to previous experimental data results.

https://orcid.org/0000-0003-0455-5401