Esterases are important enzymes in biology and biotechnology but synthetic esterases in the literature generally only hydrolyzed highly activated esters. In this work, protein sized nanoparticles were prepared with an active site containing a general base in the proximity of zinc-bound water. The shape and size of the active site were controlled by molecular imprinting within doubly cross-linked micelles. Systematic tuning of the base yielded a synthetic esterase capable of hydrolyzing nonactivated alkyl esters at neutral pH and room temperature. The catalysts displayed enzyme-like kinetics and hydrolyzed less reactive esters in the presence of more reactive ones. The catalytic efficiency and turn-over numbers were 1–2 orders of magnitude higher than the previously reported systems.

Nanoparticle-based artificial esterase with fine-tuned catalytic active sites for selective hydrolysis of esters at neutral pH and room temperature

ACS Fall 2020 Virtual Meeting

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.