Biocatalysts immobilization onto nanomaterials has been implemented into a variety of applications ranging from biosensing to biotransformation, and from decontamination to energy storage.  However, retaining enzyme catalytic activity at such nanointerfaces was challenged by either the non-specific attachment of the enzyme resulting in catalytic center deactivation at the nanointerface or increased enzyme-enzyme interactions known to lead to crosslinking and subsequent loss of enzyme activity. The next generation of enzyme-based applications need to account for increased enzyme functionality, high operational and storage stability, efficiency and yield of recovery and conversion at the nanointerface, as well as reduced enzyme inhibition.  We proposed that user-tailored control of the enzyme-nanointerface reactions could lead to enhanced enzyme catalytic efficiency. Our systematic study shows that the enzyme and the nanosupport characteristics (e.g., surface chemistry, surface charge, physical volume to surface ratio etc.) work synergistically to determine and control enzyme functionality and catalytic behavior at nanointerfaces. Further, our results show that user-tailoring the enzyme immobilization techniques at nanointerfaces could lead to robust enzyme-based nanointerfaces to be used for a variety of applications from enzyme-based biosensors to enzyme-based decontamination platforms.

Enzyme catalytic efficiency is a function of bio-nano interface reactions

248th National Meeting (2014)

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