Enhancing Catalytic Efficiency and Colloidal Stability of Nanozymes through Protein Interactions

Artificial enzyme mimics that combine protein materials and inorganic nanomaterials have great potential.

We aim to enhance their catalytic efficiency and colloidal stability by exploring the helping role of proteins in manganese oxide-based enzyme mimics and understanding the molecular origin of their catalytic specificity.Our interdisciplinary team from LU, with expertise in enzyme technology, protein interactions, manganese oxides, catalysis, structural characterisation, in-situ methods, and Monte Carlo simulation, will use state-of-the-art UV-visible, Fourier transform infrared spectro-electrochemical, electron microscopy and X-ray scattering instruments to gather crucial kinetic and structural data.This data will inform kinetic Monte Carlo models, helping us uncover the kinetics, surface heterogeneity, pattern formation, and migration of species involved in enzyme mimics´ colloidal stability and catalytic efficiency.This research is vital, as it will significantly advance our understanding of how inorganic-organic materials exhibit unique physicochemical properties due to synergistic effects from combining individual elements.

Revealing these underlying mechanisms will pave the way for more efficient and stable mimics, unlocking their full potential across various applications where natural enzymes fail.