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<p>Cascade catalysis of glutamate oxidase (GLOX) and catalase (CAT) is an important one-pot synthetic route for α-ketoglutarate (α-KG) production. However, as the soluble natural proteins, the instability of free GLOX and CAT and the difficulty of recycling severely limits its application. Here, magnetic dual-enzyme cross-linked enzyme aggregates (combi-CLEAs) of GLOX and CAT were successfully prepared with amino-functionalized Fe<sub>3</sub>O<sub>4</sub> magnetic nanoparticles as the carrier by a macromolecular cross-linking agent. Preparation conditions of the combi-CLEAs were systematically optimized. The highest activity recovery of combi-CLEAs reached 81% under the optimized conditions. Meanwhile, the combi-CLEAs exhibited high stability than free enzymes, including temperature tolerance, pH tolerance, and storage capacity. After incubation at 80&#xa0;°C for 30&#xa0;min, the magnetic combi-CLEAs retained 25% of its initial activity whereas the free enzymes maintained only 10%. Moreover, after 6 cycles of use, the combi-CLEAs maintained 74% of its initial activity, indicating excellent reusability. In particular, the combi-CLEAs exhibited high substrate tolerance and conversion efficiency of L-glutamate to α-KG. The total α-KG yield by combi-CLEAs after 6 cycles of use was 5.8 times higher than that of the free enzyme system.</p>

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Magnetic Combined Cross-Linked Enzyme Aggregates of Glutamate Oxidase and Catalase by Macromolecular Cross-Linker for Synthesis of α-Ketoglutaric Acid

  • 期刊论文

  • 发表日期：

    2026年7月1日

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  • Shumao Yang,
  • Minsong Zhang,
  • Peng Liu,
  • Linxuan Kang,
  • Jiandong Cui

摘要

Cascade catalysis of glutamate oxidase (GLOX) and catalase (CAT) is an important one-pot synthetic route for α-ketoglutarate (α-KG) production. However, as the soluble natural proteins, the instability of free GLOX and CAT and the difficulty of recycling severely limits its application. Here, magnetic dual-enzyme cross-linked enzyme aggregates (combi-CLEAs) of GLOX and CAT were successfully prepared with amino-functionalized Fe3O4 magnetic nanoparticles as the carrier by a macromolecular cross-linking agent. Preparation conditions of the combi-CLEAs were systematically optimized. The highest activity recovery of combi-CLEAs reached 81% under the optimized conditions. Meanwhile, the combi-CLEAs exhibited high stability than free enzymes, including temperature tolerance, pH tolerance, and storage capacity. After incubation at 80 °C for 30 min, the magnetic combi-CLEAs retained 25% of its initial activity whereas the free enzymes maintained only 10%. Moreover, after 6 cycles of use, the combi-CLEAs maintained 74% of its initial activity, indicating excellent reusability. In particular, the combi-CLEAs exhibited high substrate tolerance and conversion efficiency of L-glutamate to α-KG. The total α-KG yield by combi-CLEAs after 6 cycles of use was 5.8 times higher than that of the free enzyme system.