What question did this study set out to answer?

The aim is to explore the potential of lysozyme amyloid fibrils as artificial enzymes with enhanced stability and activity.

April 25, 2026ACS Applied Bio Materials0 citations

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Activation of Lysozyme with Robust Flavoenzyme Activity by Amyloid Fibrillation

AHAndi Hu CMChi Meng FFFude Feng

Key Points

The aim is to explore the potential of lysozyme amyloid fibrils as artificial enzymes with enhanced stability and activity.
Amyloid fibrils of lysozyme were engineered to bind flavin mononucleotide (FMN).
Enzyme activity was assessed by measuring NADH oxidase activity and Fe3+-cyt c reductase-like activity under various conditions.
Stability and performance were evaluated at high temperatures and in organic solvents.
FMNLAF demonstrated NADH oxidase activity with a Km of 55.3 μM and Kcat of 0.65 min-1.
At 60 °C, FMNLAF maintains enhanced enzyme activity, highlighting structural stability.
FMNLAF showed promising Fe3+-cyt c reductase activity in aerated conditions.

Abstract

The intrinsic disadvantages of natural enzymes limit their practical applications. How to achieve artificial enzymes with a green process, low cost, high stability, robust catalytic activity, and excellent biocompatibility remains a great challenge. Amyloid fibrils deserve particular attention in electron transfer and biocatalysis due to their unique biochemical properties and long-range ordered structure. Inspired by the relationship between the structure and function of natural flavoenzymes, we report that lysozyme amyloid fibril (LAF) binds cofactor flavin mononucleotide (FMN) and forms a stable nanofibril complex (FMNLAF) through noncovalent interactions. Interestingly, FMNLAF exhibits NADH oxidase activity (Km, 55.3 μM; Kcat, 0.65 min-1) to generate NAD+ under physiological conditions. Possessing exceptional structural stability, FMNLAF shows enhanced activity at high temperature (60 °C) and tolerates organic solvents. In addition, FMNLAF also exhibits strong Fe3+-cyt c reductase-like activity in aerated environments. This work provides a convenient and rational strategy for designing metal-free biocatalytic systems through amyloid fibrillation, which converts a protein into an artificial enzyme.

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Cite This Study

Hu et al. (Thu,) studied this question.

synapsesocial.com/papers/69ec5ae988ba6daa22dac7f6 https://doi.org/https://doi.org/10.1021/acsabm.6c00447

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