Researchers at Hainan University engineered a novel protein, LSUBP [el-es-ju-bi-pi], to enhance uranium extraction from seawater. This offers an alternative method for sourcing uranium, a critical element for nuclear energy production. Seawater contains about 4.5 billion tons of uranium, a virtually inexhaustible resource.
The extraction of uranium from seawater is complicated by its low concentration and competition from other dissolved metal ions. Existing adsorption-based materials have had limited success due to low efficiency and poor binding capacities. Scientists engineered LSUBP with targeted mutations, incorporating twin uranyl-binding sites.
Structural analyses confirmed that the redesigned protein retained its original conformation. Researchers constructed cross-linked hydrogel fibers that included the engineered protein. The resulting fibers showed exceptional durability, essential for practical deployment in seawater extraction.
The cross-linked LSUBP fibers displayed a uranium adsorption capacity of 25.60 mg per gram in natural seawater. Molecular docking studies validated the effectiveness of the dual uranyl-binding sites. These studies indicated that the modifications engineered into the LSUBP protein actively facilitated the high-level adsorption capacity.
Ning Wang, a lead researcher, stated that proteins rich in α-helical [alpha-helical] structures could serve as ideal platforms for engineering multiple uranyl-binding sites. This approach illuminates potential pathways for developing advanced materials aimed at extracting other essential metal ions. The research is published in the National Science Review.