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Published on: March 22, 2020
Stabilization of alkaline phosphatase with Au@Ag2O nanoparticles
Brian A Zaccheo1, Richard M Crooks
1Department of Chemistry and Biochemistry, Texas Materials Institute, and Center for Nano- and Molecular Science and Technology, The University of Texas at Austin, 1 University Station, A5300, Austin, Texas 78712-0165, USA.
Abstract:
Here, we report that a conductive Au@Ag(2)O nanoparticle structure significantly enhances the stability of alkaline phosphatase (AlkP) in the presence of the inhibitors urea and l-phenylalanine (Phe). The enzyme/nanoparticle construct is prepared by associating the enzyme with citrate-capped Au particles, and then adding Ag(+). UV-vis and XPS spectroscopy and transmission electron microscopy confirm the core@shell structure. AlkP activity was quantified in the presence and absence of the two inhibitors using a time-resolved colorimetric assay. The results indicate that 21% of the initial active AlkP is incorporated into the nanoparticle structure. More importantly, however, the Au@Ag(2)O core@shell host reduces the inhibitory effect of urea and Phe by factors ranging from 3 to 12, depending on the inhibitor and its concentration, compared to the wild-type enzyme.

