Biotransformation of (1-phenyl)ethyl hydroperoxide with Aspergillus niger: a model study on enzyme selectivity and on the induction of peroxidase activity

• Published in: Biochimica et biophysica acta Vol. 1427; no. 2; pp. 236 - 244
• Main Authors: Adam, Waldemar, Lukacs, Zoltan, Saha-Möller, Chantu R, Schreier, Peter
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 19.04.1999
• Subjects: (1-Phenyl)ethyl hydroperoxide; Aspergillus niger; Aspergillus niger - enzymology; biosynthesis; Biotransformation; Catalase; Catalase - metabolism; Cations, Divalent; Cold Temperature; Enantioselectivity; Enzyme induction; enzymology; Fungal Proteins; Fungal Proteins - biosynthesis; gene induction; induction; Kinetics; metabolism; Oxidation-Reduction; Peroxidase; Peroxidase - biosynthesis; Peroxidase - metabolism; peroxidases; peroxides; Peroxides - metabolism; Stereoisomerism; Stress response; Peroxidase; Enantioselectivity; (1-Phenyl)ethyl hydroperoxide; Stress response; Aspergillus niger; Enzyme induction
• ISSN: 0304-4165; 0006-3002; 1872-8006; 1878-2434
• DOI: 10.1016/S0304-4165(99)00019-7

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 Fe 2+, Mn 2+ and Zn 2+ in the growth medium, since the addition of Fe 2+ ions substantially (threefold) increases the enantioselectivity, whereas addition of Mn 2+ and Zn 2+ ions decreases it. Finally, the cold shock (4°C) significantly enhances the reduction of the hydroperoxide by the microorganism A. niger.