ArticleHeliyon2023
Chitosan-Based metal-organic framework for Stabilization of β-glucosidase: Reusability and storage stability.
Article in Heliyon, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 27 citations in OpenAlex.
- Review
- Biocomposites of Enzymes and Covalent Organic Frameworks: A Novel Family of Heterogenous Biocatalysis.Chem & bio engineering · 2025Review
- Article
- An Overview of Microorganisms Immobilized in a Gel Structure for the Production of Precursors, Antibiotics, and Valuable Products.Gels (Basel, Switzerland) · 2024Review
- NiNanoscale advances · 2024Article
- Sustainable Immobilization of β-Glucosidase onto Silver Ions and AgNPs-Loaded Acrylic Fabric with Enhanced Stability and Reusability.Polymers · 2023Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Enzyme immobilization is a powerful tool for protecting enzymes from harsh reaction conditions and improving enzyme activity, stability, and reusability. In this study, metal organic frameworks (MIL-Fe composites) were synthesized via solvothermal reactions and then modified with chitosan (CS). β-Glucosidase was immobilized on the chitosan-metal organic framework (CS-MIL-Fe), and the resulting composites were characterized with various analytical techniques. The β-glucosidase immobilized on a CS-MIL-Fe composite had an immobilization yield of 85 % and a recovered activity of 74 %. The immobilized enzyme retained 81 % of its initial activity after ten successive cycles and preserved 69 % of its original activity after 30 days of storage at 4 °C. In contrast, the free enzyme had only preserved 32 % of its original activity after 30 days. Under various temperature and pH conditions, the immobilized enzyme showed greater stability than the free enzyme, and the optimal temperature and pH were 60 °C and 6.0 for the immobilized enzyme and 50 °C and 5.0 for the free enzyme. The kinetic parameters were also determined, with the Km values of 13.4 and 6.98 mM for the immobilized and free β-glucosidase, respectively, and Vmax values of 3.96 and 1.72 U/mL, respectively. Overall, these results demonstrate that the CS-MIL-Fe@β-glucosidase is a promising matrix showing high catalytic efficiency and enhanced stability.
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Registered trials
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