LAUSR

Oligomeric proteins are abundant in nature. However, their synthesis remains a significant challenge. A controlled oligomerization process can provide important insights into the evolution of modern proteins and the development of more efficient biocatalysts. Here, we propose a pathway for producing glucose oxidase (GOx) homooligomer (Ol-GOx), a redox enzyme with extensive biotechnological applications. We obtained Ol-GOx from the one-pot reaction of the native protein with a Bronsted acid, trifluoromethanesulfonic acid (TFMS). Ol-GOx had a hydrodynamic radius of 96 nm and a molecular mass of 2 MDa. Ol-GOx exhibited higher thermal stability in comparison to the native protein, as well as increased hydrophobicity, which is a primary characteristic needed for its stabilization in the solid state for applications in bioenergy, heterogeneous catalysis, and biomedicine. Furthermore, there were remarkable improvements in redox properties and protein stabilization, suggesting that this approach for Ol-GOx synthe...