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Novel Siloxane Derivatives as Membrane Precursors for Lactate Oxidase Immobilization.

ABSTRACT: We report new enzyme-containing siloxane membranes for biosensor elaboration. Lactate oxidase immobilization from water-organic mixtures with a high concentration of organic solvent (90%) leads to advanced lactate biosensors. The use of the new alkoxysilane monomers-(3-aminopropyl)trimethoxysilane (APTMS) and trimethoxy[3-(methylamino)propyl]silane (MAPS)-as the base for enzyme-containing membrane construction resulted in a biosensor with up to a two times higher sensitivity (0.5 A·M^-1·cm^-2) compared to the biosensor based on (3-aminopropyl)triethoxysilane (APTES) we reported previously. The validity of the elaborated lactate biosensor for blood serum analysis was shown using standard human serum samples. The developed lactate biosensors were validated through analysis of human blood serum.

SUBMITTER: Vokhmyanina DV

PROVIDER: S-EPMC10145638 | biostudies-literature | 2023 Apr

REPOSITORIES: biostudies-literature

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Novel Siloxane Derivatives as Membrane Precursors for Lactate Oxidase Immobilization.

Vokhmyanina Darya V DV Sharapova Olesya E OE Buryanovataya Ksenia E KE Karyakin Arkady A AA

Sensors (Basel, Switzerland) 20230415 8

We report new enzyme-containing siloxane membranes for biosensor elaboration. Lactate oxidase immobilization from water-organic mixtures with a high concentration of organic solvent (90%) leads to advanced lactate biosensors. The use of the new alkoxysilane monomers-(3-aminopropyl)trimethoxysilane (APTMS) and trimethoxy[3-(methylamino)propyl]silane (MAPS)-as the base for enzyme-containing membrane construction resulted in a biosensor with up to a two times higher sensitivity (0.5 A·M<sup>-1</sup ...[more]

PMID: 37112357

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Project description:Immobilization of enzymes on (nano)porous metal carriers provides the foundation for an advanced design of bioelectrodes suitable for catalysis and sensing. However, interactions upon adsorption are still poorly understood, and so the efficient coupling of the enzymes to the electrode surface remains one of the major challenges. Here, we present a comprehensive study of the immobilization behavior of Aerococcus viridans l-lactate oxidase (LOx) on nanoporous gold (npAu) in dependence of electrode modification with differently charged self-assembled monolayers (SAMs). The highest activity (up to 14 U/g) and electrocatalytic response (sensitivity of 3.9 μA mM-1) were observed for a sulfonate-terminated SAM. This is contrary to enzyme behavior on conventional polymer carriers, and thus, the effect is specific to the metal electrodes. We propose the capture of the negatively charged LOx in a dense counterion layer in close proximity to the strongly negatively charged gold surface. Adsorption on positively charged amine-terminated SAMs resulted in a similar immobilization yield but gave much lower activity (4-fold). Importantly, the effect of the sulfonate SAM was strongly dependent on the npAu electrode pore size: the highest LOx activity (in U/cm2) was found with pores (diameter of ∼170 nm) supposedly large enough to facilitate enzyme diffusion into the porous structure during immobilization. Electrochemical sensing of H2O2 produced by the LOx reaction showed a 2.5-fold higher sensitivity for l-lactate on the negatively charged surface. Lixiviation studies supported the proposed layer capture and revealed a faster decline in the electrode activity with sulfonate surface modification. Collectively, the present study reveals enhanced activity of LOx on sulfonate-charged gold surfaces and a strong pore size dependence. These findings deepen the understanding of the immobilization behavior of LOx on charged nanoporous metals and have importance for the advanced design of enzyme electrodes.

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Novel Siloxane Derivatives as Membrane Precursors for Lactate Oxidase Immobilization.

Publications

Novel Siloxane Derivatives as Membrane Precursors for Lactate Oxidase Immobilization.

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