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Updated: Feb 17, 2026

Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability
Published on: April 22, 2016
Co-immobilization of enoate reductase with a cofactor-recycling partner enzyme
Han Li1, Wenhua Xiao1, Panpan Xie1
1Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, College of Life Sciences, Jilin University, Changchun 130012, People's Republic of China.
Abstract:
Herein we established co-immobilized methods for enoate reductases (ERs) and glucose dehydrogenase (GDH), forming a cofactor regeneration system. In cross-linked enzyme aggregates (CLEAs), ammonium sulfate and oxidized dextran were selected as a precipitant and a cross-linker, respectively. In biomimetic immobilization (BI), ER-GDH-silica particles (ER-GDH-SPs) were rapidly formed through a one-step approach by using a silicic acid precursor. Under the optimal conditions, the ER activity recovery in ER-GDH-CLEAs and ER-GDH-SPs were 44.9±1.8% and 44.5±2.1%, and the immobilization efficiency was 93.5±1.2% and 92.4±1.2%, respectively. ER-GDH-CLEAs and ER-GDH-SPs exhibit excellent thermal and pH stability, and superior reusability. The activity of ER-GDH-SPs toward the substrate is also better than that of free ER and GDH in reduction of 4-(4-Methoxyphenyl)-3-buten-2-one. This study introduces simple and inexpensive co-immobilization strategies to construct novel and efficient ER-GDH-CLEAs and ER-GDH-SPs with high activity and stability.
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