Biotransformation of (1-phenyl)ethyl hydroperoxide with Aspergillus niger: a model study on enzyme selectivity and on the induction of peroxidase activity.
The biocatalytic enantioselective reduction of (1-phenyl)ethyl hydroperoxide (1) by the fungus Aspergillus niger to the corresponding alcohol 2 involves a multi-enzyme biotransformation of the hydroperoxide 1, as revealed by the change in the enantioselectivity as a function of incubation times. This unusual behavior is not exhibited by other fungi and seems to be restricted to A. niger. Furthermore, the peroxidase and other oxidoreductase activities of A. niger depend on the availability of metal ions such as Fe2+, Mn2+ and Zn2+ in the growth medium, since the addition of Fe2+ ions substantially (threefold) increases the enantioselectivity, whereas addition of Mn2+ and Zn2+ ions decreases it. Finally, the cold shock (4 degrees C) significantly enhances the reduction of the hydroperoxide by the microorganism A. niger.
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Institute of Organic Chemistry, University of Würzburg, Am Hubland, D-97074, Würzburg, Germany. adam@chemie.uni-wuerzburg.de
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Saha-Möller
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Schreier
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D001234:Aspergillus niger / Q000201:enzymology*; D001711:Biotransformation; D002374:Catalase / Q000378:metabolism; D002413:Cations, Divalent; D003080:Cold Temperature; D005656:Fungal Proteins / Q000096:biosynthesis; D007700:Kinetics; D010084:Oxidation-Reduction; D009195:Peroxidase / Q000096:biosynthesis / Q000378:metabolism*; D010545:Peroxides / Q000378:metabolism*; D013237:Stereoisomerism
D002413:Cations, Divalent; D005656:Fungal Proteins; D010545:Peroxides; C041000:ethylbenzene hydroperoxide; D002374:Catalase; D009195:Peroxidase