Work

SpyCatcher-Multiplicity Tunes Nanoscaffold Hydrogels for Enhanced Catalysis of Regulated Enzymes

Year: 2025

Type: article

Abstract: This study presents a strategy for enhancing hydrogel formation through SpyCatcher-mediated conjugation of nanoscale scaffold proteins. We demonstrate that SpyCatcher can facilitate hydrogel assembly with various nano-scaffolds of diverse structural configurations. By conjugating one, two, or three SpyCatcher units to the P9 protein nanoscaffold, hydrogel yield was substantially increased, allowing for the simultaneous co-immobilization of a larger number of enzymes. Characterization using cell-free biosynthesis, electron microscopy, and rheological analysis revealed that the resulting SpyCatcher-mediated nanoscaffold hydrogels exhibit soft solid-like behavior, high elasticity, and an “ink-bottle” pore morphology, which collectively promote and regulate enzymatic activity. Notably, hydrogels crosslinked via the P9 scaffold with two SpyCatcher units showed the most balanced properties, leading to a 149% increase in pyruvic acid production. These findings not only advance the efficient design of hydrogels for enzyme co-immobilization but also provide a foundation for developing more sophisticated models and expanding the scope of biocatalytic systems.

Source: Processes

DOI: 10.3390/pr13124009

Authors: Xue Yin, Bei Liao, Hui Li, Ming-Yue Huang, Fu-Xing Niu

Institutions: Guangxi University of Science and Technology, Guangxi Key Laboratory of Green Processing of Sugar Resources

Language: English

Topic: Enzyme Catalysis and Immobilization

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: gold

Estimated APC paid: $2,896

Funders: National Natural Science Foundation of China, Guangxi University, Guangxi University of Science and Technology