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Enhancing recombinant urate oxidase stability and catalytic function with TMAO osmolyte: integrated experimental and computational approaches
Abstract Compatible osmolytes like trimethylamine N-oxide (TMAO), known for preferentially stabilizing proteins in their folded states, offer a potential solution; however, the precise molecular mechanisms underlying their stabilizing effects are not fully understood. On the other hand, the poor thermal stability of pharmaceutical enzymes such as urate oxidase (UOX) in aqueous solutions remains a significant challenge.
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