Issue 31, 2024

Co-immobilization of a bi-enzymatic cascade into hierarchically porous MIL-53 for efficient 6′-sialyllactose production

Abstract

6′-Sialyllactose (6′-SL), the most abundant sialylated human milk oligosaccharide, has attracted attention for its potential application in supplementary infant formulas. Herein, we report a facile strategy to construct a cascade bioreactor for the enzymatic synthesis of 6′-SL by co-immobilizing an enzymatic module consisting of CMP–sialic acid synthase and α-2,6-sialyltransferase into hierarchically porous MIL-53 (HP-MIL-53). The as-prepared HP-MIL-53 showed high enzyme immobilization capacity, reaching 226 mg g−1. Furthermore, the co-immobilized enzymes exhibited higher initial catalytic efficiency, and thermal, pH and storage stability than the free ones. Finally, the 6′-SL yield remained >80% after 13 cycles of use. We expect that HP-MIL-53 would have potential industrial applications in the enzymatic modular synthesis of 6′-SL and other glycans.

Graphical abstract: Co-immobilization of a bi-enzymatic cascade into hierarchically porous MIL-53 for efficient 6′-sialyllactose production

Supplementary files

Article information

Article type
Paper
Submitted
24 Apr 2024
Accepted
11 Jul 2024
First published
24 Jul 2024

Nanoscale, 2024,16, 14932-14939

Co-immobilization of a bi-enzymatic cascade into hierarchically porous MIL-53 for efficient 6′-sialyllactose production

X. Peng, C. Pei, E. W. Qian, Y. Du and J. Li, Nanoscale, 2024, 16, 14932 DOI: 10.1039/D4NR01775G

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