Discovery and Characterization of a 5-Hydroxymethylfurfural Oxidase from Methylovorus

نویسندگان

  • Willem P. Dijkman
  • Marco W. Fraaije
چکیده

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منابع مشابه

Discovery and characterization of a 5-hydroxymethylfurfural oxidase from Methylovorus sp. strain MP688.

In the search for useful and renewable chemical building blocks, 5-hydroxymethylfurfural (HMF) has emerged as a very promising candidate, as it can be prepared from sugars. HMF can be oxidized to 2,5-furandicarboxylic acid (FDCA), which is used as a substitute for petroleum-based terephthalate in polymer production. On the basis of a recently identified bacterial degradation pathway for HMF, ca...

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Creating a more robust 5-hydroxymethylfurfural oxidase by combining computational predictions with a novel effective library design

Background HMF oxidase (HMFO) from Methylovorus sp. is a recently characterized flavoprotein oxidase. HMFO is a remarkable enzyme as it is able to oxidize 5-hydroxymethylfurfural (HMF) into 2,5-furandicarboxylic acid (FDCA): a catalytic cascade of three oxidation steps. Because HMF can be formed from fructose or other sugars and FDCA is a polymer building block, this enzyme has gained interest ...

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Creating Oxidase–Peroxidase Fusion Enzymes as a Toolbox for Cascade Reactions

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Enzymatic Preparation of 2,5-Furandicarboxylic Acid (FDCA)—A Substitute of Terephthalic Acid—By the Joined Action of Three Fungal Enzymes

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, ...

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تاریخ انتشار 2017