ArticleMolecules (Basel, Switzerland)2017
New Heterofunctional Supports Based on Glutaraldehyde-Activation: A Tool for Enzyme Immobilization at Neutral pH.
Article in Molecules (Basel, Switzerland), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Innovative Immobilization ofJournal of agricultural and food chemistry · 2026Article
- Immobilization of a Fungal Fructosyltransferase onto Silica Gel and Glutaraldehyde-Functionalized Silica Gel for Biocatalytic Applications.ACS omega · 2026Article
- Kinetic and thermodynamic studies on the thermal inactivation of lipase immobilized on glutaraldehyde-activated rice husk silica.Biotechnology letters · 2024Article
- Structural Studies ofInternational journal of molecular sciences · 2023Article
- Multienzyme Coimmobilization on Triheterofunctional Supports.Biomacromolecules · 2023Article
- Immobilization and Application of the Recombinant Xylanase GH10 ofInternational journal of molecular sciences · 2022Article
- Microbial Lipases and Their Potential in the Production of Pharmaceutical Building Blocks.International journal of molecular sciences · 2022Review
- Multiplatform Protein Detection and Quantification Using Glutaraldehyde-Induced Fluorescence for 3D Systems.Journal of fluorescence · 2019Article
- New Strategy for the Immobilization of Lipases on Glyoxyl-Agarose Supports: Production of Robust Biocatalysts for Natural Oil Transformation.International journal of molecular sciences · 2017Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Immobilization is an exciting alternative to improve the stability of enzymatic processes. However, part of the applied covalent strategies for immobilization uses specific conditions, generally alkaline pH, where some enzymes are not stable. Here, a new generation of heterofunctional supports with application at neutral pH conditions was proposed. New supports were developed with different bifunctional groups (i.e., hydrophobic or carboxylic/metal) capable of adsorbing biocatalysts at different regions (hydrophobic or histidine richest place), together with a glutaraldehyde group that promotes an irreversible immobilization at neutral conditions. To verify these supports, a multi-protein model system (
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