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- W1120931337 abstract "Abstract The purpose of this work is to study the adsorption process and surface bio-activity of His-tagged d -amino acid oxidase (DAAO) from Rhodotorula gracilis (His 6 - Rg DAAO) as the first step for the development of an electrochemical bio-functionalized platform. With such a purpose this work comprises: (a) the His 6 - Rg DAAO bio-activity in solution determined by amperometry, (b) the adsorption mechanism of His 6 - Rg DAAO on bare gold and carboxylated modified substrates in the absence (substrate/COO − ) and presence of Ni(II) (substrate/COO − + Ni(II)) determined by reflectometry, and (c) the bio-activity of the His 6 - Rg DAAO bio-functionalized platforms determined by amperometry. Comparing the adsorption behavior and bio-activity of His 6 - Rg DAAO on these different solid substrates allows understanding the contribution of the diverse interactions responsible for the platform performance. His 6 - Rg DAAO enzymatic performance in solution is highly improved when compared to the previously used pig kidney ( pk ) DAAO. His 6 - Rg DAAO exhibits an amperometrically detectable bio-activity at concentrations as low as those expected on a bio-functional platform; hence, it is a viable bio-recognition element of d -amino acids to be coupled to electrochemical platforms. Moreover, His 6 - Rg DAAO bio-functionalized platforms exhibit a higher surface activity than pk DAAO physically adsorbed on gold. The platform built on Ni(II) modified substrates present enhanced bio-activity because the surface complexes histidine–Ni(II) provide with site-oriented, native-like enzymes. The adsorption mechanism responsible of the excellent performance of the bio-functionalized platform takes place in two steps involving electrostatic and bio-affinity interactions whose prevalence depends on the degree of surface coverage." @default.
- W1120931337 created "2016-06-24" @default.
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- W1120931337 date "2015-11-01" @default.
- W1120931337 modified "2023-10-08" @default.
- W1120931337 title "d -Amino acid oxidase bio-functionalized platforms: Toward an enhanced enzymatic bio-activity" @default.
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- W1120931337 doi "https://doi.org/10.1016/j.apsusc.2015.08.121" @default.
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