Abstract
Flavoprotein oxidases utilize the naturally abundant flavin adenosine dinucleotide (FAD) or flavin mononucleotide (FMN) as cofactors to shuttle hydrogen atoms and electrons between their specific substrates and molecular oxygen. As such, flavoprotein oxidases are valuable biocatalysts in industrial applications because of their ability to use molecular oxygen as a clean and free oxidant. These enzymes are known to oxidize CO, CN, and CS bonds. Flavoprotein oxidases, such as hydroxymethylfurfural oxidase, glucose oxidase, pyranose 2-oxidase, d-amino acid oxidase, and cholesterol oxidase, have been used as industrial biocatalysts.
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