ArticleMolecules (Basel, Switzerland)2019
Co-Immobilization of Tri-Enzymes for the Conversion of Hydroxymethylfurfural to 2,5-Diformylfuran.
Article in Molecules (Basel, Switzerland), 2019. 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, 30 citations in OpenAlex.
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- Green synthesis of magnetic bio-Graphene nanohybrid for the immobilization of hydrolytic enzymes towards sustainable bioconversion of cellulose.RSC advances · 2025Article
- Enzyme-Mediated Alleviation of Peroxide Toxicity in Self-Oxygenating Biomaterials.Advanced healthcare materials · 2022Article
- Bromelain and Nisin: The Natural Antimicrobials with High Potential in Biomedicine.Pharmaceutics · 2021Review
- Prospects of Using Biocatalysis for the Synthesis and Modification of Polymers.Molecules (Basel, Switzerland) · 2021Review
- Preparation of 1-Hydroxy-2,5-hexanedione from HMF by the Combination of Commercial Pd/C and Acetic Acid.Molecules (Basel, Switzerland) · 2020Article
- Editorial for Special Issue: Enzyme Immobilization and Its Applications.Molecules (Basel, Switzerland) · 2019Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Acting as a "green" manufacturing route, the enzyme toolbox made up of galactose oxidase, catalase, and horseradish peroxidase can achieve a satisfactory yield of 2,5-diformylfuran derived from 30 mM hydroxymethylfurfural. However, as the concentration of hydroxymethylfurfural increases, the substrate causes oxidative damage to the activity of the tri-enzyme system, and the accumulated hydrogen peroxide produced by galactose oxidase causes tri-enzyme inactivation. The cost of tri-enzymes is also very high. These problems prevent the utilization of this enzyme toolbox in practice. To address this, galactose oxidase, catalase, and horseradish peroxidase were co-immobilized into Cu
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Registered trials
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