Characterisation of recombinant pyranose oxidase from the cultivated mycorrhizal basidiomycete <Emphasis Type="Italic">Lyophyllum shimeji</Emphasis> (hon-shimeji) |
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| Authors: | Clara Salaheddin Yoshimitsu Takakura Masako Tsunashima Barbara Stranzinger Oliver Spadiut Montarop Yamabhai Clemens K Peterbauer Dietmar Haltrich |
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| Institution: | (1) Food Biotechnology Laboratory, Department of Food Science and Technology, BOKU University of Natural Resources and Life Sciences, Vienna, Austria;(2) Research Centre Applied Biocatalysis, Graz, Austria;(3) Plant Innovation Center, Japan Tobacco, Iwata, Shizuoka, Japan;(4) School of Biotechnology, Suranaree University of Technology, Nakhon Ratchasima |
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| Abstract: | 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. |
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