Home Institute: Università di Pavia, Italy
Main supervisor: Andrea Mattevi
Co-Supervisors: Silvia Osuna (UGD) and
Ferran Fancho (ZYM)
Required academic background: Chemistry, Biochemistry, Structural Biology, and Biophysics or related.

This project will focus on the design, screening, structural and functional characterization of enzymes acting on nylon. They will be engineered using structure-based tools. Fusions will be created for the most effective amidase mutants with peptides known for their efficient nylon binding. The study will include biophysical and crystallographic studies focusing on enzymes bound to amide-oligomers or monomers. Additionally, cryo-electron microscopy will determine the structure of the fused peptide-fused amidase (nylonase) enzymes when bound to polyamide polymers.

Objectives:

  • Design and screening of enzymes acting on nylon.
  • Biophysical characterization of binding kinetics, binding density, and depolymerization kinetics, analysis and crystallographic studies on the enzyme in complex with amide-oligomer(s) or monomer(s).
  • Structure determination of the peptide-fused amidase (nylonase) enzymes bound to the polyamide polymers using cryo-electron microscopy.

Expected results:

  • Novel enzymes for polyamide degradation.
  • Guide further optimization of the amidase and polymer-binding peptides feeding the activities of DC8.
  • Unprecedented knowledge about the structural principles underlying enzyme-polymer recognition.