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Background  The flavin-dependent enzyme pyranose 2-oxidase (P2Ox) has gained increased attention during the last years because of a number of attractive applications for this enzyme. P2Ox is a unique biocatalyst with high potential for biotransformations of carbohydrates and in synthetic carbohydrate chemistry. Recently, it was shown that P2Ox is useful as bioelement in biofuel cells, replacing glucose oxidase (GOx), which traditionally is used in these applications. P2Ox offers several advantages over GOx for this application, e.g., its much broader substrate specificity. Because of this renewed interest in P2Ox, knowledge on novel pyranose oxidases isolated from organisms other than white-rot fungi, which represent the traditional source of this enzyme, is of importance, as these novel enzymes might differ in their biochemical and physical properties.    Results  We isolated and over-expressed the  p2ox  gene encoding P2Ox from the ectomycorrhizal fungus  Lyophyllum shimeji . The  p2ox  cDNA was inserted into the bacterial expression vector pET21a(+) and successfully expressed in  E. coli  Rosetta 2. We obtained active, flavinylated recombinant P2Ox in yields of approximately 130 mg per L of medium. The enzyme was purified by a two-step procedure based on anion exchange chromatography and preparative native PAGE, yielding an apparently homogenous enzyme preparation with a specific activity of 1.92 U/mg (using glucose and air oxygen as the substrates). Recombinant P2Ox from  L. shimeji  was characterized in some detail with respect to its physical and catalytic properties, and compared to the well-characterised enzymes from  Phanerochaete chrysosporium  and  Trametes multicolor .    Conclusion   L. shimeji  P2Ox shows properties that are comparable to those of P2Ox from white-rot fungal origin, and is in general characterised by lower K m  and  k  cat  values both for electron donor (sugar) as well as electron acceptor (ferrocenium ion, 1,4-benzoquinone, 2,6-dichloroindophenol). While  L. shimeji  P2Ox is the least thermostable of these three enzymes (melting temperature  T  m  of 54.9°C; half-life time of activity τ 1/2  of 0.12 at 50°C and pH 6.5),  P. chrysosporium  P2Ox showed remarkable thermostability with  T  m  of 75.4°C and τ 1/2  of 96 h under identical conditions.

Characterisation of recombinant pyranose oxidase from the cultivated mycorrhizal basidiomycete Lyophyllum shimeji (hon-shimeji)