| About this Abstract |
| Meeting |
2023 TMS Annual Meeting & Exhibition
|
| Symposium
|
Bio-Nano Interfaces and Engineering Applications
|
| Presentation Title |
Self-assembled Flavoprotein Putrescine Oxidase System Offers Enhanced Thermal Stability |
| Author(s) |
Taylor Bader, Emina Derakovic , Nilan J. B. Kamathewatta, Chris Johnson, Cindy L. Berrie, Candan Tamerler |
| On-Site Speaker (Planned) |
Taylor Bader |
| Abstract Scope |
Flavoprotein putrescine oxidase belonging to the oxidoreductase family are considered valuable biocatalysts. These enzymes catalyze the oxidation of a wide range of compounds simultaneously reducing oxygen to hydrogen peroxide. Putrescine oxidase is a polyamine related to cell growth and differentiation processes, and provides critical information when used as diagnostic enzymes, cancer biomarkers, or for monitoring food freshness due to amino acid degradation. Orientation control to display the active site is necessary to maintain the activity of immobilized enzymes. Their deeply buried active site brings an additional challenge for providing an optimal catalytic interface. Here we investigate guiding the supramolecular self-assembly of putrescine oxidase using a peptide tag at this complex bionanomaterial interface. Functionalized surfaces were analyzed using combined characterization including SPR and QCM-D as well as enzyme activity measurements and cyclic voltammetry. Our results revealed that the immobilized enzymes maintained their catalytic activity while exhibiting improved reusability and thermal stability. |
| Proceedings Inclusion? |
Planned: |
| Keywords |
Surface Modification and Coatings, Thin Films and Interfaces, Biomaterials |