Professor Marc-Olivier Coppens at the Rensselaer Polytechnic Institute has created a method to enhance enzyme stability, enabling their use in more applications. He trapped enzymes that included lysozyme in carefully created nanopores. It was revealed that these embedded enzymes became more active while retaining their original structure.
Coppens embedded enzymes into nanopores. Lysozyme measures 3 to 4nm in size and can be comfortably fitted into the nanoporous material of controlled pore size, which measure between 5 and 12nm. The narrow space makes it hard for the enzymes to move or wriggle around. The research could impact biology, chemistry, healthcare, and nanoengineering.
The research paper has been co-authored by former graduate in the Department of Chemical and Biological Engineering at the institute Lung-Ching Sang. The research paper, ‘Effects of surface curvature and surface chemistry on the structure and activity of proteins adsorbed in nanopores,’ has appeared in Physical Chemistry Chemical Physics.
This National Science Foundation supported the research through the Nanoscale Science and Engineering Center for Directed Assembly of Nanostructures at Rensselaer. The International Center for Materials Nanoarchitectonics of the National Institute for Materials Science in Japan has also supported the program.