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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]
Copyright of Journal of Biotechnology is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Engineering Source
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Header DbId: egs
DbLabel: Engineering Source
An: 190988254
AccessLevel: 6
PubType: Academic Journal
PubTypeId: academicJournal
PreciseRelevancyScore: 0
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Items – Name: Title
  Label: Title
  Group: Ti
  Data: Sodium alginate-immobilized epoxide hydrolase: A multifaceted strategy for enhanced stability, reusability, and catalytic performance.
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  Data: <searchLink fieldCode="AR" term="%22Yu%2C+Zongzhong%22">Yu, Zongzhong</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Zhu%2C+Meinan%22">Zhu, Meinan</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Gu%2C+Xiao%22">Gu, Xiao</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Wu%2C+Zhongkun%22">Wu, Zhongkun</searchLink><relatesTo>2</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Chen%2C+Peiqin%22">Chen, Peiqin</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Jin%2C+Chunying%22">Jin, Chunying</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Zhao%2C+Junning%22">Zhao, Junning</searchLink><relatesTo>3</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Zhang%2C+Guangya%22">Zhang, Guangya</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Jiang%2C+Wei%22">Jiang, Wei</searchLink><relatesTo>1</relatesTo> (AUTHOR)<i> wjiang@hqu.edu.cn</i>
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  Data: <searchLink fieldCode="JN" term="%22Journal+of+Biotechnology%22">Journal of Biotechnology</searchLink>. Feb2026, Vol. 410, p84-95. 12p.
– Name: Subject
  Label: Subjects
  Group: Su
  Data: <searchLink fieldCode="DE" term="%22Sodium+alginate%22">Sodium alginate</searchLink><br /><searchLink fieldCode="DE" term="%22Epoxide+hydrolase%22">Epoxide hydrolase</searchLink><br /><searchLink fieldCode="DE" term="%22Biocompatibility%22">Biocompatibility</searchLink><br /><searchLink fieldCode="DE" term="%22Immobilized+enzymes%22">Immobilized enzymes</searchLink><br /><searchLink fieldCode="DE" term="%22Enzyme+regulation%22">Enzyme regulation</searchLink><br /><searchLink fieldCode="DE" term="%22Mathematical+optimization%22">Mathematical optimization</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: 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]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Journal of Biotechnology is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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RecordInfo BibRecord:
  BibEntity:
    Identifiers:
      – Type: doi
        Value: 10.1016/j.jbiotec.2025.11.017
    Languages:
      – Code: eng
        Text: English
    PhysicalDescription:
      Pagination:
        PageCount: 12
        StartPage: 84
    Subjects:
      – SubjectFull: Sodium alginate
        Type: general
      – SubjectFull: Epoxide hydrolase
        Type: general
      – SubjectFull: Biocompatibility
        Type: general
      – SubjectFull: Immobilized enzymes
        Type: general
      – SubjectFull: Enzyme regulation
        Type: general
      – SubjectFull: Mathematical optimization
        Type: general
    Titles:
      – TitleFull: Sodium alginate-immobilized epoxide hydrolase: A multifaceted strategy for enhanced stability, reusability, and catalytic performance.
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            NameFull: Yu, Zongzhong
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            NameFull: Zhu, Meinan
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            NameFull: Gu, Xiao
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            NameFull: Wu, Zhongkun
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            NameFull: Chen, Peiqin
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            NameFull: Jin, Chunying
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            NameFull: Zhao, Junning
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            NameFull: Zhang, Guangya
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            – D: 01
              M: 02
              Text: Feb2026
              Type: published
              Y: 2026
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            – Type: issn-print
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              Value: 410
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