Alizarin is an anti-fungal compound produced by the plant, Rubia tinctorum. The parasitic fungus Bjerkandera adusta Dec 1 was cultured in potato dextrose (PD) medium with or without alizarin. Alizarin was a good substrate for the dye-decolorizing peroxidase (DyP) from B. adusta Dec 1 and hampered B. adusta growth at the early stage of plate culture. During liquid shaking culture, DyP activity in cultures supplemented with 100 μM alizarin was greater than that in controls cultured without alizarin. In particular, DyP activity per dry cell mass increased approximately 3.5-, 3.1-, and 2.9-fold at 24, 30, and 36 h after inoculation, respectively, compared with control cultures. These data suggest that alizarin stimulates the expression of DyP. Interestingly, alizarin rapidly decomposed at an early stage in culture (24-42 h) in PD medium supplemented with 100 μM alizarin. Thus, alizarin appears to induce DyP expression in B. adusta Dec 1, and this DyP, in turn, rapidly degrades alizarin. Collectively, our findings suggest that the physiological role of DyP is to degrade antifungal compounds produced by plants.
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http://dx.doi.org/10.1186/s13568-019-0779-4 | DOI Listing |
Microbiol Resour Announc
January 2023
Department of Chemical and Biological Sciences, Faculty of Science, Japan Women's University, Tokyo, Japan.
We report the draft genome sequence of Bjerkandera adusta Dec 1, a basidiomycete that was isolated from the soil in Yokohama, Japan, using the Illumina HiSeq platform. B. adusta Dec 1 was identified as a fungus that degrades persistent anthraquinone dyes, and the novel peroxidase DyP was responsible for this degradation.
View Article and Find Full Text PDFMolecules
January 2021
Department of Lifestyle Disorders and Regenerative Medicine, University of Information Technology and Management in Rzeszow, Sucharskiego Street 2, 35-225 Rzeszow, Poland.
The aim of this study was to evaluate the bioremoval mechanism of anthracycline antibiotics by the white-rot fungus CCBAS 930. The activity of oxidoreductases and levels of phenolic compounds and free radicals were determined during the biotransformation of anthraquinone antibiotics: daunomycin (DNR) and doxorubicin (DOX) by strain CCBAS 930. Moreover, phytotoxicity ( L.
View Article and Find Full Text PDFWorld J Microbiol Biotechnol
December 2020
Department of Environmental Microbiology, Laboratory of Mycology, The University of Life Sciences, Leszczyńskiego Street 7, 20-069, Lublin, Poland.
We used a ligninolytic strain of the white-rot fungus B. adusta CCBAS 930 and its mutants with modified ligninolytic activity to assess their potential to remove of molasses. The analyzed strains have been shown to be able to decolorize 1% or 2% molasses solutions containing brown-colored toxic melanoidins.
View Article and Find Full Text PDFEnzyme Microb Technol
December 2019
Centro de Nanociencias y Nanotecnología, Universidad Nacional Autónoma de México, Ensenada, Baja California, Mexico. Electronic address:
Versatile peroxidase (VP) from Bjerkandera adusta is an enzyme able to oxidize bulky and high-redox substrates trough a Long-Range Electron Transfer (LRET) pathway. In this study, the introduction of radical-forming aromatic amino acids by chemical modification of the protein surface was performed, and the catalytic implications of these additional surface active-sites on the oxidation of 2,6-dimethylphenol, Mn and Remazol Brilliant Blue R (RBBR) were determined. These three different substrates are oxidized in different active-sites of enzyme molecule, of which the high redox RBBR the only one that is transformed by an external radical formed on the protein surface.
View Article and Find Full Text PDFAMB Express
April 2019
Department of Chemical and Biological Sciences, Faculty of Science, Japan Women's University, 2-8-1 Mejirodai, Bunkyo-ku, Tokyo, 112-8681, Japan.
Alizarin is an anti-fungal compound produced by the plant, Rubia tinctorum. The parasitic fungus Bjerkandera adusta Dec 1 was cultured in potato dextrose (PD) medium with or without alizarin. Alizarin was a good substrate for the dye-decolorizing peroxidase (DyP) from B.
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