Spatial distribution and proximity effect-dependent multi-enzyme cascades catalysis operating in dendritic mesoporous silica nanoparticles

Abstract

Enzymatic cascades catalysis engenders complex and selective intracellular transformations due to the organization of the enzymes in confined cellular environments. In this work, a biomimetic strategy is employed to develop a synthetic cell analogue for operating multi-enzymatic cascade catalysis in vitro. The glucose peroxidase (GOx) and chloroperoxidase (CPO) are co-encapsulated in the channel of dendritic mesoporous silica nanoparticles (DMSP) modified by phase-transitioned lysozyme (PTL@GOx&CPO@DMSP). The cascade efficiency is substantially enhanced compared with the diffusion mixtures of the free enzymes in bulk solution due to some nanoscale construction, such as confinement effect, proximity effect and special distribution mode of the enzymes. The high specific surface area and high concentration of mesoporous cages in DMSP is beneficial for encapsulation of enzyme. The cross-linked cavities ensure directional transfer of the intermediate from GOx to CPO, known as “substrate channel”. PTL plays multiple functions including inhibiting leaking of enzyme from DMSP, concentrating intermediate H2O2 at DMSP domains and keeping this biocomposite stable in aqueous environment by improving its dispersibility. The prepared biocomposite PTL@GOx & CPO@DMSP is very stable at harsh conditions. It can retain 42% of original catalytic activity at 90°C with incubation for 3 h while the retained activity of free enzymes is only 5% under the same conditions. Meanwhile, it can keep 92.4% of its original catalytic activity after 10 reuses. These characteristics ensure practical application of this biocatalytic material. The active HClO generated by GOx-CPO cascade has an efficient anti-tumor effect and is effectively applied to preserve fruit.