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Which is the physiological function of Pyranose 2-oxidase from phanaerocite chrysosporium and trametes vescicolor? 


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Pyranose 2-oxidase (POx) from Phanerochaete chrysosporium and Trametes versicolor plays a crucial role in lignocellulose degradation. These enzymes oxidize aldopyranoses in lignocellulose to 2-ketoaldoses, aiding in the breakdown of complex plant material. The active site of POx is essential for efficient binding of both electron-donor substrates (sugars) and electron-acceptor substrates (oxygen or quinone compounds) during the oxidative half-reaction. Additionally, POx shows a wide substrate specificity, making it valuable for various biotechnological applications. The enzyme's ability to catalyze the oxidation of sugars to 2-ketoaldoses suggests its involvement in lignin degradation processes, highlighting its physiological function in lignocellulose breakdown.

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