Induction of manganese peroxidase and laccase by Lentinula edodes under liquid culture conditions and their isozyme detection by enzymatic staining on native-PAGE

• Published in: Mycoscience Vol. 52; no. 2; pp. 132 - 136
• Main Authors: Saeki, Naomi, Takeda, Hironori, Tanesaka, Eiji, Yoshida, Motonobu
• Format: Journal Article
• Language: English
• Published: Japan Elsevier B.V 01.03.2011; Japan : Springer Japan; Springer Japan
• Subjects: Biomedical and Life Sciences; Biotechnology; Breeding; Castanopsis cuspidata; Copper ion; Enzymes; Eukaryotic Microbiology; Extracellular enzyme; Gel electrophoresis; Inoculation; Isoenzymes; Laccase; Lentinula edodes; Life Sciences; Liquid culture; Manganese peroxidase; Mass spectroscopy; Media (culture); Microbial Ecology; Microbiology; Phenoloxidase; Phenoloxidases; Sawdust; Shiitake mushroom; Short Communication; Shiitake mushroom; Copper ion; Breeding; Extracellular enzyme; Phenoloxidases
• ISSN: 1340-3540; 1618-2545
• DOI: 10.1007/S10267-010-0076-1

The white-rot basidomycete Lentinula edodes often produces the lignin-degrading enzymes manganese peroxidase (MnP; EC 1.11.1.13) and laccase (Lcc; EC 1.10.3.2) in sawdust-based media. In the present study, MnP from L. edodes was induced under liquid culture supplemented with sawdust extracts of Castanopsis cuspidata. Lcc activity was induced by the addition of 2mM CuSO4 5H2O into the same media 7 days after initial inoculation. Phenoloxidase enzymes were distinguished by polyacrylamide gel electrophoresis (native- PAGE), followed by sequential enzymatic staining with an improved staining solution. The isozyme bands detected under MnP-induced conditions were identified as manganese peroxidase (lemnp2) and bands detected under Lcc-induced conditions were identified as laccase (lcc1) by Q-TOF mass spectrometry.