ArticleBiomacromolecules2023
Multienzyme Coimmobilization on Triheterofunctional Supports.
Article in Biomacromolecules, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 20 citations in OpenAlex.
- Sequential Conjugation of Two Different Types of Catalytically Active Enzymes to Liposomes via Bis-Aryl Hydrazone Bonds.ACS omega · 2026Article
- Oppositely Charged Single Enzyme Nanogels Form Versatile Coacervates for Efficient Enzyme Cascade Catalysis.Advanced materials (Deerfield Beach, Fla.) · 2026Article
- Immobilized Hydroxymethylfurfural Oxidase Enables Robust Biocatalytic Production of 2,5-Furandicarboxylic Acid from Crude 5‑Hydroxymethylfurfural.ACS sustainable chemistry & engineering · 2026Article
- A Multi-Functional Heterogeneous Biocatalyst for the Oxygen-Free Oxidative Condensation of Primary Alcohols into β‑Hydroxy Acids.ACS catalysis · 2026Article
- Immobilization of Thrombin on Agarose-Based Supports for Affinity Tag Removal.Biomacromolecules · 2025Article
- Optimized Spatial Configuration of Heterogeneous Biocatalysts Maximizes Cell-Free Biosynthesis of ω-Hydroxy and ω-Amino Acids.ACS sustainable chemistry & engineering · 2024Article
- Interactive biocatalysis achieved by driving enzyme cascades inside a porous conducting material.Communications chemistry · 2024Review
- Engineered repeat proteins as scaffolds to assemble multi-enzyme systems for efficient cell-free biosynthesis.Nature communications · 2023Article
Corrections and comments
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Immobilized multienzyme systems are gaining momentum in applied biocatalysis; however, the coimmobilization of several enzymes on one carrier is still challenging. In this work, we exploited a heterofunctional support activated with three different chemical functionalities to immobilize a wide variety of different enzymes. This support is based on agarose microbeads activated with aldehyde, amino, and cobalt chelate moieties that allow a fast and irreversible immobilization of enzymes, enhancing the thermostability of most of the heterogeneous biocatalysts (up to 21-fold higher than the soluble one). Furthermore, this trifunctional support serves to efficiently coimmobilize a multienzyme system composed of an alcohol dehydrogenase, a reduced nicotinamide adenine dinucleotide (NADH) oxidase, and a catalase. The confined multienzymatic system demonstrates higher performance than its free counterpart, achieving a total turnover number (TTN) of 1 × 10
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.