Production of Hydroxy Acids: Selective Double Oxidation of Diols by Flavoprotein Alcohol Oxidase. Issue 12 (4th February 2020)

• Record Type: Journal Article
• Authors: Martin, Caterina; Trajkovic, Milos; Fraaije, Marco W.
• Is Part Of: Angewandte Chemie international edition. Volume 59:Issue 12(2020)
• Page Start: 4869
• Page End: 4872
• Publication Date: 2020-02-04
• Subjects: biocatalysis -- diols -- enzymes -- lactones -- oxidation; Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201914877
• Languages: English
• ISSNs: 1433-7851

Abstract

Abstract: Flavoprotein oxidases can catalyze oxidations of alcohols and amines by merely using molecular oxygen as the oxidant, making this class of enzymes appealing for biocatalysis. The FAD‐containing (FAD=flavin adenine dinucleotide) alcohol oxidase from P. chrysosporium facilitated double and triple oxidations for a range of aliphatic diols. Interestingly, depending on the diol substrate, these reactions result in formation of either lactones or hydroxy acids. For example, diethylene glycol could be selectively and fully converted into 2‐(2‐hydroxyethoxy)acetic acid. Such a facile cofactor‐independent biocatalytic route towards hydroxy acids opens up new avenues for the preparation of polyester building blocks. Abstract : Triple action : The flavoprotein alcohol oxidase (AOX*) facilitates the double and triple oxidations of diols. Interestingly, depending on the diol substrate, these reactions result in formation of either lactones or hydroxy acids. Such biocatalytic route towards hydroxy acids has potential for the preparation of polyester building blocks.