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. 2018 Jun 15;4(6):eaat2816.
doi: 10.1126/sciadv.aat2816. eCollection 2018 Jun.

Biomimetic enzyme cascade reaction system in microfluidic electrospray microcapsules

Huan Wang  1 , Ze Zhao  1 , Yuxiao Liu  1 , Changmin Shao  1 , Feika Bian  1 , Yuanjin Zhao  1
Affiliations

Biomimetic enzyme cascade reaction system in microfluidic electrospray microcapsules

Huan Wang et al. Sci Adv. .

Abstract

Mimicking subcellular compartments containing enzymes in organisms is considered a promising approach to substitute for missing or lost cellular functions. Inspired by the multicompartment structures of cellular architectures, we present a novel multienzyme system based on hollow hydrogel microcapsules with flexible enzymatic inverse opal particles. Benefiting from the precise operation capability of the microfluidic electrospray and the remarkable structural color marks in the inverse opal particles, we developed a multienzyme system with controllable number, type, and spatial arrangement of the encapsulated enzymes. The hydrogel shells also could improve enzyme stability against proteolysis in the system. The multienzyme system containing alcohol oxidase and catalase could act as a cascade biocatalyst and reduce alcohol levels in media, providing an alternative antidote and prophylactic for alcohol intoxication. These features indicated that our strategy provides an ideal enzyme cascade reaction system for complex biocatalysis and biomimetic functions of some organelles or organs.

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Figures

Fig. 1
Fig. 1. Schematics of the preparation of the bioinspired microcapsules.
(A) Schematic of the enzyme cascade reaction in a cell. (B) Schematic of the enzyme cascade reaction in the microcapsule encapsulated with enzyme-immobilized inverse opal particles. (C) Schematic of the microcapsule generation process with the microfluidic electrospray.
Fig. 2
Fig. 2. SEM images and metalloscope images of the inverse opal particles.
(A) The surface and (B) the inner side of an inverse opal particle with a higher concentration of the cross-linker. (C to E) Reflection images of the green, red, and blue inverse opal particles. (F) Reflection peaks and reflection images of five different inverse opal particles. RP, reflective percent. Scale bars, 500 nm (A), 2 μm (B), and 100 μm (C to E).
Fig. 3
Fig. 3. The stereomicroscope images of the microcapsules with different cores.
(A to C) One core. (D and E) Two cores. (F) Three cores. Scale bars, 400 μm.
Fig. 4
Fig. 4. The catalytic activity of the microcapsules.
(A) Catalytic activity of HRP microcapsules and free HRP particles before and after treatment with trypsin. (B) Catalytic capability of the β-G–, GOD-, and HRP-immobilized inverse opal particles with and without encapsulations.
Fig. 5
Fig. 5. Biocatalysis of the microcapsules during the cell culture.
(A to C) Fluorescent staining of the cells (A) in alcohol mixed medium, (B) in the mixed medium of alcohol and AOx-encapsulated microcapsules, and (C) in the mixed medium of alcohol and AOx/Cat co-encapsulated microcapsules. (D) Corresponding cell viabilities. Scale bars, 50 μm.
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