Researchers at Rensselaer Polytechnic Institute Discover New Method To Boost Enzymatic Activity
Proteins are critically important to life and the human body. They are also among the most complex molecules in nature, and there is much we still don’t know or understand about them.
One key challenge is the stability of enzymes, a particular type of protein that speeds up, or catalyzes, chemical reactions. Taken out of their natural environment in the cell or body, enzymes can quickly lose their shape and denature. Everyday examples of enzymes denaturing include milk going sour, or eggs turning solid when boiled.
Rensselaer researchers confined lysozyme and other enzymes inside carefully engineered nanoscale holes. Instead of denaturing, these embedded enzymes mostly retained their 3-D structure and exhibited a significant increase in activity. Copyright Rensselaer Polytechnic Institute
Rensselaer Polytechnic Institute Professor Marc-Olivier Coppens has developed a new technique for boosting the stability of enzymes, making them useful under a much broader range of conditions. Coppens confined lysozyme and other enzymes inside carefully engineered nanoscale holes, or nanopores. Instead of denaturing, these embedded enzymes mostly retained their 3-D structure and exhibited a significant increase in activity.
Read full press release: http://news.rpi.edu/update.do?artcenterkey=2851
Read the PCCP paper:
Effects of surface curvature and surface chemistry on the structure and activity of proteins adsorbed in nanopores
Lung-Ching Sang and Marc-Olivier Coppens
Phys. Chem. Chem. Phys., 2011, 13, 6689-6698
