With land-based uranium supplies dwindling, scientists are turning to the sea. Now, a breakthrough from China’s Hainan University may have cracked the code for extracting this critical fuel from seawater—thanks to a genetically engineered protein that binds uranium like a magnet. Findings from the new study were published recently in the National Science Review.
A team of researchers at Hainan University has engineered a novel protein, dubbed LSUBP, that could revolutionize how we harvest uranium from the ocean. Designed with precision genetic tweaks, LSUBP contains two uranyl-binding sites that dramatically improve the protein’s ability to adsorb uranium—making it one of the most effective materials ever developed for this purpose.
Uranium is the lifeblood of nuclear power, but terrestrial reserves are finite. By contrast, Earth’s oceans are a veritable uranium vault, containing an estimated 4.5 billion tons of the element in low concentrations. The problem? It’s dissolved at just 3.3 parts per billion, and competing metal ions make it notoriously hard to isolate.
The Hainan team tackled this by strategically mutating a naturally stable protein to include dual binding pockets specifically tuned to latch onto uranyl ions. These “twin sites” were incorporated without disrupting the protein’s overall architecture—a key achievement confirmed by structural analysis.
To test their innovation in real-world conditions, the scientists embedded the LSUBP protein into cross-linked hydrogel fibers. The result: a tough, reusable material capable of pulling uranium directly from natural seawater.
When deployed, the fibers achieved an adsorption capacity of 25.60 milligrams of uranium per gram of material. That’s a significant leap over previous biomolecular or synthetic adsorbents. Just as importantly, the hydrogel remained stable and effective after multiple uses, a critical metric for commercial feasibility.
Behind the scenes, molecular docking simulations validated what the experiments showed—the dual uranyl-binding sites actively engage with uranium ions, driving the high efficiency observed.
The implications stretch beyond uranium. By applying similar engineering strategies, researchers could design proteins that extract other valuable metals from the sea or from industrial wastewater.
“Numerous proteins naturally rich in α-helical structures could serve as ideal platforms for engineering multiple uranyl-binding sites,” said Ning Wang, a lead researcher on the project. “By applying the genetic engineering strategy, we can rationally design additional specific binding sites, significantly enhancing the uranium extraction capabilities of protein-based adsorbents from seawater."
The work opens new doors for sustainable nuclear fuel sourcing and advances the broader field of bio-based metal recovery technologies—transforming proteins into the next generation of molecular miners.
With land-based uranium supplies dwindling, scientists are turning to the sea. Now, a breakthrough from China’s Hainan University may have cracked the code for extracting this critical fuel from seawater—thanks to a genetically engineered protein that binds uranium like a magnet. Findings from the new study were published recently in the National Science Review.
A team of researchers at Hainan University has engineered a novel protein, dubbed LSUBP, that could revolutionize how we harvest uranium from the ocean. Designed with precision genetic tweaks, LSUBP contains two uranyl-binding sites that dramatically improve the protein’s ability to adsorb uranium—making it one of the most effective materials ever developed for this purpose.
Uranium is the lifeblood of nuclear power, but terrestrial reserves are finite. By contrast, Earth’s oceans are a veritable uranium vault, containing an estimated 4.5 billion tons of the element in low concentrations. The problem? It’s dissolved at just 3.3 parts per billion, and competing metal ions make it notoriously hard to isolate.
The Hainan team tackled this by strategically mutating a naturally stable protein to include dual binding pockets specifically tuned to latch onto uranyl ions. These “twin sites” were incorporated without disrupting the protein’s overall architecture—a key achievement confirmed by structural analysis.
To test their innovation in real-world conditions, the scientists embedded the LSUBP protein into cross-linked hydrogel fibers. The result: a tough, reusable material capable of pulling uranium directly from natural seawater.
When deployed, the fibers achieved an adsorption capacity of 25.60 milligrams of uranium per gram of material. That’s a significant leap over previous biomolecular or synthetic adsorbents. Just as importantly, the hydrogel remained stable and effective after multiple uses, a critical metric for commercial feasibility.
Behind the scenes, molecular docking simulations validated what the experiments showed—the dual uranyl-binding sites actively engage with uranium ions, driving the high efficiency observed.
The implications stretch beyond uranium. By applying similar engineering strategies, researchers could design proteins that extract other valuable metals from the sea or from industrial wastewater.
“Numerous proteins naturally rich in α-helical structures could serve as ideal platforms for engineering multiple uranyl-binding sites,” said Ning Wang, a lead researcher on the project. “By applying the genetic engineering strategy, we can rationally design additional specific binding sites, significantly enhancing the uranium extraction capabilities of protein-based adsorbents from seawater."
The work opens new doors for sustainable nuclear fuel sourcing and advances the broader field of bio-based metal recovery technologies—transforming proteins into the next generation of molecular miners.