|About this Abstract
||2018 TMS Annual Meeting & Exhibition
||Bio-nano Interfaces and Engineering Applications Symposium
||Self-assembled Formate Dehydrogenase-metal Nanoparticle Hybrids Improved Enzyme Stability
||Rachel Lietz, Sarah VanOosten, Erkan Mozioglu, Brandon Tomas, Kasra Alizadeh, Mark Richter, Candan Tamerler
|On-Site Speaker (Planned)
Formate dehydrogenase (FDH) plays a critical role in regenerating NADH and producing methanol and formic acid, which can be used as precursors to novel fuels and chemicals. Despite its great potential, FDH has limited industrial use due to its low stability and lack of reusability thus there is significant interest in immobilization of this enzyme. Current methods involves mainly covalent immobilization of enzymes, which jeopardize enzymatic function by altering its optimum configuration in addition to involving harsh chemicals. Here we utilize a metal binding peptide (MtBP) to functionalize formate dehydrogenase (FDH) onto the surface of gold nanoparticles. We verified binding and enzyme activity on the gold nanoparticles using L-SPR and UV-Vis spectroscopic analyses, respectively. Finally enzymatic stability was monitored over a range of temperature and pH values. The engineered FDH with peptide tag could be used as a robust biocatalyst system for biomedical and energy applications.
||Planned: Publication Outside of TMS (Indicate publication title and publisher if known.)