ArticleThe protein journal2026
Expression, Purification, and Characterization of Recombinant Isocitrate Dehydrogenase (IDH) from Yarrowia lipolytica and its Application as a Protein Template for In Situ Synthesis of Gold Nanoparticles.
Article in The protein journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
In this study, isocitrate dehydrogenase (IDH) was employed exclusively as a structural protein template for the synthesis of gold nanoparticles, rather than relying on its enzymatic catalytic function. The reduction of Au³⁺ to Au⁰ is accomplished through the intrinsic reducing capability of amino acid residues (particularly tryptophan and tyrosine) within the protein scaffold, which simultaneously acts as a capping and stabilizing agent. This protein-templating strategy provides a straightforward, biocompatible, and cofactor-free approach for developing AuNP-based biosensing platforms. So, the IDH-based AuNPs offers promising applications across medical diagnostics, environmental monitoring, food safety, and research. In this study, we produced the recombinant isocitrate dehydrogenase of Yarrowia lipolytica yeast in E. coli BL21. After optimizing the enzyme activity/stability in the proper pH and temperature, its activity was then measured with K
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