Abstract
Multiple enzyme coimmobilizations mimicking nature cascade enzymatic pathways have potential applications in diverse fields. We have developed a strategy for orderly coimmobilizing multienzymes by combining hierarchically self-assembled multimeric enzymes with specifically abundant polyhistidine tag affinity-mediated immobilization. Using this strategy, an ordered coimmobilization of the glycosyltransferase UGT51 mutant and sucrose synthase was constructed to realize the regeneration of costly sugar donor UDP-glucose that was used in the biosynthesis of the rare ginsenoside Rh2. The ordered coimmobilization array not only significantly boosted the immobilization and catalysis efficiency but also improved UDP-glucose regeneration, storage stability, and reusability compared to those of random coimmobilization and free enzyme-assembly systems. This study provides a great promise for fabricating enzyme arrays and highlights the synergistic benefits of nanocomplexes in enhancing biocatalytic cascade performance.
| Original language | English |
|---|---|
| Pages (from-to) | 3027-3034 |
| Number of pages | 8 |
| Journal | ACS Applied Bio Materials |
| Volume | 4 |
| Issue number | 4 |
| DOIs | |
| State | Published - 19 Apr 2021 |
| Externally published | Yes |
Bibliographical note
Publisher Copyright:© 2021 American Chemical Society.
Keywords
- coimmobilizations
- glycosyltransferase
- multimeric enzymes
- self-assembly
- sucrose synthase
- UDP-glucose regeneration
ASJC Scopus subject areas
- Biomaterials
- General Chemistry
- Biomedical Engineering
- Biochemistry, medical
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