State Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing 100190, China.
Key Laboratory of Biopharmaceutical Preparation and Delivery, Chinese Academy of Sciences, Beijing 100190, China.
Nanoscale. 2024 Aug 13;16(31):14932-14939. doi: 10.1039/d4nr01775g.
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. 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.
6'-唾液乳糖（6'-SL）是最丰富的人乳寡糖唾液酸化形式，因其在补充婴儿配方中的潜在应用而受到关注。在此，我们报告了一种简便的策略，通过将包含 CMP-唾液酸合酶和 α-2,6-唾液酸转移酶的酶模块共固定到分级多孔 MIL-53（HP-MIL-53）中，构建用于酶促合成 6'-SL 的级联生物反应器。所制备的 HP-MIL-53 表现出高的酶固定化能力，达到 226mg g-1。此外，共固定化酶表现出比游离酶更高的初始催化效率、热稳定性、pH 稳定性和储存稳定性。最后，在 13 次使用循环后，6'-SL 的产率仍保持在>80%。我们期望 HP-MIL-53 在 6'-SL 和其他糖的酶促模块合成中具有潜在的工业应用。
