Scalable purification of High Purity Recombinant Lanthanide Ion Selective Protein from Methylorubrum extorquens and metal binding affinities

Authors

Presenter(s)

Courtney Henthorn

Comments

Presentation: 1:40-2:00 p.m., Kennedy Union 222

Files

Description

I will be discussing a novel purification method for isolating the lanthanide-sequestering protein, Lanmodulin, from an E.coli expression process, in addition to discussing comparative metal binding affinities of Lanmodulin to Europium(III) and Iron(III). This research topic is of major interest due to the unfulfilled demand for a national, sustainable supply of rare earth elements (REEs), for applications such as permanent magnets, energy storage devices, biomining, and metal waste valorization. My findings include a reproducible and scalable purification method for the isolation of His6-tagged LanM, its resulting activity compared to a LanM purified using a published method, and confirmation that heat treatment does not hinder the metal binding properties of LanM nor reduce the yield of the LanM.

Publication Date

4-19-2023

Project Designation

Honors Thesis

Primary Advisor

Justin Biffinger

Primary Advisor's Department

Chemistry

Keywords

Stander Symposium, College of Arts and Sciences

Institutional Learning Goals

Scholarship; Critical Evaluation of Our Times

Recommended Citation

"Scalable purification of High Purity Recombinant Lanthanide Ion Selective Protein from Methylorubrum extorquens and metal binding affinities" (2023). Stander Symposium Projects. 2791.
https://ecommons.udayton.edu/stander_posters/2791