# Sucrose Monolaurate as a Stabilizer for Lactate Oxidase Electrodes at Low pH: A Structural Analysis Based on Grazing Incidence Small-Angle X‑ray Scattering

## TL;DR

This paper shows how a sugar surfactant called sucrose monolaurate helps protect lactate oxidase enzymes on electrodes in acidic conditions.

## Contribution

The study reveals the structural mechanism of enzyme stabilization using grazing incidence small-angle X-ray scattering.

## Key findings

- Sucrose monolaurate helps retain 80% enzyme activity at pH 5.0.
- GI-SAXS shows enzyme is embedded in hexagonal and lamellar structures.
- Encapsulation protects enzymes without blocking substrate access.

## Abstract

Sugars and sugar surfactants can increase the storage
stability
of enzyme electrodes. In this study, the feasibility of using sugar
surfactants as stabilizers for enzyme electrode operation under acidic
conditions was investigated along with their stabilizing mechanism.
Lactate oxidase (LOx)–sucrose monolaurate-modified electrodes
maintained ∼80% of their activity at pH 5.0, compared with
∼50% activity retention without a stabilizer. To elucidate
the stabilizing mechanism, the structure of sucrose monolaurate with
and without LOx on common electrode materials was analyzed using grazing
incidence small-angle X-ray scattering (GI-SAXS). The results revealed
that LOx was embedded in hexagonal arrangements and lamellar structures
comprising sucrose monolaurate. Encapsulation protected the microenvironment
of the enzyme against pH changes, without hindering its access to
the substrate and mediator. This study confirms the high potential
utility of GI-SAXS as a powerful tool for elucidating the structure-derived
mechanisms of enzyme-electrode modifications.