Enzymatic oxidation of 5-hydroxymethylfurfural (HMF) and its oxidized derivatives was studied using three fungal enzymes: wild-type aryl alcohol oxidase (AAO) from three fungal species, wild-type peroxygenase from Agrocybe aegerita (AaeUPO), and recombinant galactose oxidase (GAO). The effect of pH on different reaction steps was evaluated and apparent kinetic data (Michaelis-Menten constants, turnover numbers, specific constants) were calculated for different enzyme-substrate ratios and enzyme combinations. Finally, the target product, 2,5-furandicarboxylic acid (FDCA), was prepared in a multi-enzyme cascade reaction combining three fungal oxidoreductases at micro-scale. Furthermore, an oxidase-like reaction is proposed for heme-containing peroxidases, such as UPO, horseradish peroxidase, or catalase, causing the conversion of 5-formyl-2-furancarboxylic acid into FDCA in the absence of exogenous hydrogen peroxide.
Identifer | oai:union.ndltd.org:DRESDEN/oai:qucosa:de:qucosa:30914 |
Date | 25 April 2018 |
Creators | Karich, Alexander, Kleeberg, Sebastian B., Ullrich, René, Hofrichter, Martin |
Publisher | Multidisciplinary Digital Publishing Institute (MDPI) |
Source Sets | Hochschulschriftenserver (HSSS) der SLUB Dresden |
Language | English |
Detected Language | English |
Type | doc-type:article, info:eu-repo/semantics/article, doc-type:Text |
Rights | info:eu-repo/semantics/openAccess |
Relation | 10.3390/microorganisms6010005 |
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