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Sodium alginate-immobilized epoxide hydrolase: A multifaceted strategy for enhanced stability, reusability, and catalytic performance.

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Title: Sodium alginate-immobilized epoxide hydrolase: A multifaceted strategy for enhanced stability, reusability, and catalytic performance.
Authors: Yu, Zongzhong1 (AUTHOR), Zhu, Meinan1 (AUTHOR), Gu, Xiao1 (AUTHOR), Wu, Zhongkun2 (AUTHOR), Chen, Peiqin1 (AUTHOR), Jin, Chunying1 (AUTHOR), Zhao, Junning3 (AUTHOR), Zhang, Guangya1 (AUTHOR), Jiang, Wei1 (AUTHOR) wjiang@hqu.edu.cn
Source: Journal of Biotechnology. Feb2026, Vol. 410, p84-95. 12p.
Subjects: Sodium alginate, Epoxide hydrolase, Biocompatibility, Immobilized enzymes, Enzyme regulation, Mathematical optimization
Abstract: Immobilized macromolecular enzymes effectively address critical challenges including environmental sensitivity, thermal instability, and non-reusability, thereby establishing the fundamental and practical significance of enzyme immobilization research. This study employed sodium alginate (SA), ZIF-8, and Bi-EA materials to immobilize Aspergillus carlsbadensis -derived epoxide hydrolase (AcEH). Comparative analysis revealed SA's superior immobilization efficiency. Material characterization via SEM, FTIR, and XRD was performed, followed by optimization of SA immobilization parameters. The immobilized enzyme maintained activity over 6 reuse cycles. Incorporating 0.5 wt% carboxymethyl cellulose (CMC) extended AcEH@SA-CMC reusability to 8 cycles. Magnetic modification through Fe 3 O 4 powder incorporation yielded AcEH@SA-CMC- Fe 3 O 4 hydrogel with enhanced recoverability. Results demonstrate SA's exceptional biocompatibility underpins its immobilization efficacy, while CMC co-entanglement creates a porous network facilitating mass transfer and mechanical reinforcement. Fe 3 O 4 powder plays a promoting role in improving enzyme activity. This methodology not only evaluates immobilization matrices but establishes an optimized protocol for macromolecular AcEH immobilization. • Comparison and exploration of various methods to immobilize the Ac EH to improve its reusability. • SA, ZIF-8, and Bi-EA materials were used to immobilize the enzyme Ac EH. • The good immobilization effect of SA on the enzyme is due to its excellent biocompatibility. • Fe 3 O 4 powder plays a promoting role in improving enzyme activity. • This section compares the effects of different immobilization methods. [ABSTRACT FROM AUTHOR]
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Database: Engineering Source
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Abstract:Immobilized macromolecular enzymes effectively address critical challenges including environmental sensitivity, thermal instability, and non-reusability, thereby establishing the fundamental and practical significance of enzyme immobilization research. This study employed sodium alginate (SA), ZIF-8, and Bi-EA materials to immobilize Aspergillus carlsbadensis -derived epoxide hydrolase (AcEH). Comparative analysis revealed SA's superior immobilization efficiency. Material characterization via SEM, FTIR, and XRD was performed, followed by optimization of SA immobilization parameters. The immobilized enzyme maintained activity over 6 reuse cycles. Incorporating 0.5 wt% carboxymethyl cellulose (CMC) extended AcEH@SA-CMC reusability to 8 cycles. Magnetic modification through Fe 3 O 4 powder incorporation yielded AcEH@SA-CMC- Fe 3 O 4 hydrogel with enhanced recoverability. Results demonstrate SA's exceptional biocompatibility underpins its immobilization efficacy, while CMC co-entanglement creates a porous network facilitating mass transfer and mechanical reinforcement. Fe 3 O 4 powder plays a promoting role in improving enzyme activity. This methodology not only evaluates immobilization matrices but establishes an optimized protocol for macromolecular AcEH immobilization. • Comparison and exploration of various methods to immobilize the Ac EH to improve its reusability. • SA, ZIF-8, and Bi-EA materials were used to immobilize the enzyme Ac EH. • The good immobilization effect of SA on the enzyme is due to its excellent biocompatibility. • Fe 3 O 4 powder plays a promoting role in improving enzyme activity. • This section compares the effects of different immobilization methods. [ABSTRACT FROM AUTHOR]
ISSN:01681656
DOI:10.1016/j.jbiotec.2025.11.017