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Yasushi Sugano - One of the best experts on this subject based on the ideXlab platform.
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Degradation of antifungal anthraquinone compounds is a probable physiological role of DyP secreted by Bjerkandera adusta
SpringerOpen, 2019Co-Authors: Kanako Sugawara, Etsuno Igeta, Yoshimi Amano, Mayuko Hyuga, Yasushi SuganoAbstract:Abstract 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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degradation of the synthetic dye amaranth by the fungus Bjerkandera adusta dec 1 inference of the degradation pathway from an analysis of decolorized products
Biodegradation, 2011Co-Authors: Nichina Gomi, Shuji Yoshida, Kazutsugu Matsumoto, Masayuki Okudomi, Hiroki Konno, Toru Hisabori, Yasushi SuganoAbstract:We examined the degradation of amaranth, a representative azo dye, by Bjerkandera adusta Dec 1. The degradation products were analyzed by high performance liquid chromatography (HPLC), visible absorbance, and electrospray ionization time-of-flight mass spectroscopy (ESI-TOF-MS). At the primary culture stage (3 days), the probable reaction intermediates were 1-aminonaphthalene-2,3,6-triol, 4-(hydroxyamino) naphthalene-1-ol, and 2-hydroxy-3-[2-(4-sulfophenyl) hydrazinyl] benzenesulfonic acid. After 10 days, the reaction products detected were 4-nitrophenol, phenol, 2-hydroxy-3-nitrobenzenesulfonic acid, 4-nitrobenzene sulfonic acid, and 3,4′-disulfonyl azo benzene, suggesting that no aromatic amines were created. Manganese-dependent peroxidase activity increased sharply after 3 days culture. Based on these results, we herein propose, for the first time, a degradation pathway for amaranth. Our results suggest that Dec 1 degrades amaranth via the combined activities of peroxidase and hydrolase and reductase action.
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degradation of the synthetic dye amaranth by the fungus Bjerkandera adusta dec 1 inference of the degradation pathway from an analysis of decolorized products
Biodegradation, 2011Co-Authors: Nichina Gomi, Shuji Yoshida, Kazutsugu Matsumoto, Masayuki Okudomi, Hiroki Konno, Toru Hisabori, Yasushi SuganoAbstract:We examined the degradation of amaranth, a representative azo dye, by Bjerkandera adusta Dec 1. The degradation products were analyzed by high performance liquid chromatography (HPLC), visible absorbance, and electrospray ionization time-of-flight mass spectroscopy (ESI-TOF-MS). At the primary culture stage (3 days), the probable reaction intermediates were 1-aminonaphthalene-2,3,6-triol, 4-(hydroxyamino) naphthalene-1-ol, and 2-hydroxy-3-[2-(4-sulfophenyl) hydrazinyl] benzenesulfonic acid. After 10 days, the reaction products detected were 4-nitrophenol, phenol, 2-hydroxy-3-nitrobenzenesulfonic acid, 4-nitrobenzene sulfonic acid, and 3,4′-disulfonyl azo benzene, suggesting that no aromatic amines were created. Manganese-dependent peroxidase activity increased sharply after 3 days culture. Based on these results, we herein propose, for the first time, a degradation pathway for amaranth. Our results suggest that Dec 1 degrades amaranth via the combined activities of peroxidase and hydrolase and reductase action.
Ulrich Szewzyk - One of the best experts on this subject based on the ideXlab platform.
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sulfophthalimide as major metabolite formed from sulfonated phthalocyanine dyes by the white rot fungus Bjerkandera adusta
Fems Microbiology Letters, 2001Co-Authors: Annette Heinflingweidtmann, Thorsten Reemtsma, Thomas Storm, Ulrich SzewzykAbstract:The reaction products formed during the decolorization of the sulfophthalocyanine textile dyes Reactive blue 15 (RB15) and Reactive blue 38 (RB38) by the white-rot fungus Bjerkandera adusta were analyzed by high-performance liquid chromatography with diode array detection and with liquid chromatography–electrospray ionization–tandem mass spectrometry. Sulfophthalimides (SPI; 3 and 4) were identified as major metabolites by comparison with synthesized reference compounds. SPI was formed from both dyes in fungal cultures and by incubation with its purified manganese peroxidase and lignin peroxidase. Quantitative assessment of the SPI formed from RB15 accounted for approximately 60% of the theoretical amount.
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purification and characterization of peroxidases from the dye decolorizing fungus Bjerkandera adusta
Fems Microbiology Letters, 1998Co-Authors: Annette Heinfling, Ángel T. Martínez, María Jesús Martínez, Matthias Bergbauer, Ulrich SzewzykAbstract:A peroxidase oxidizing Mn2+ (MnP) is described for the first time in Bjerkandera adusta, a fungus efficiently degrading xenobiotic compounds. The MnP appeared as two isoenzymes, which were purified to homogeneity together with two lignin peroxidases (LiP). Their N-terminal sequences were identical, but the MnP isoenzymes showed more basic isoelectric points and differences in amino acid composition and catalytic properties. The B. adusta LiP is similar to LiP from Phanerochaete chrysosporium. However, the interest of the MnP described here is related to its ability to catalyze Mn2+-mediated as well as Mn2+-independent reactions on aromatic compounds, which may be of use for applications in biotechnology and environmental technology.
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transformation of industrial dyes by manganese peroxidases from Bjerkandera adusta and pleurotus eryngii in a manganese independent reaction
Applied and Environmental Microbiology, 1998Co-Authors: Annette Heinfling, Ángel T. Martínez, María Jesús Martínez, Matthias Bergbauer, Ulrich SzewzykAbstract:We investigated the transformation of six industrial azo and phthalocyanine dyes by ligninolytic peroxidases from Bjerkandera adusta and other white rot fungi. The dyes were not oxidized or were oxidized very little by Phanerochaete chrysosporium manganese peroxidase (MnP) or by a chemically generated Mn3+-lactate complex. Lignin peroxidase (LiP) from B. adusta also showed low activity with most of the dyes, but the specific activities increased 8- to 100-fold when veratryl alcohol was included in the reaction mixture, reaching levels of 3.9 to 9.6 U/mg. The B. adusta and Pleurotus eryngii MnP isoenzymes are unusual because of their ability to oxidize aromatic compounds like 2,6-dimethoxyphenol and veratryl alcohol in the absence of Mn2+. These MnP isoenzymes also decolorized the azo dyes and the phthalocyanine complexes in an Mn2+-independent manner. The reactions with the dyes were characterized by apparent Km values ranging from 4 to 16 μM and specific activities ranging from 3.2 to 10.9 U/mg. Dye oxidation by these peroxidases was not increased by adding veratryl alcohol as it was in LiP reactions. Moreover, the reaction was inhibited by the presence of Mn2+, which in the case of Reactive Black 5, an azo dye which is not oxidized by the Mn3+-lactate complex, was found to act as a noncompetitive inhibitor of dye oxidation by B. adusta MnP1.
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biodegradation of azo and phthalocyanine dyes by trametes versicolor and Bjerkandera adusta
Applied Microbiology and Biotechnology, 1997Co-Authors: Annette Heinfling, Matthias Bergbauer, Ulrich SzewzykAbstract:Eighteen fungal strains, known for their ability to degrade lignocellulosic material or lignin derivatives, were screened for their potential to decolorize commercially used reactive textile dyes. Three azo dyes, Reactive Orange 96, Reactive Violet 5 and Reactive Black 5, and two phthalocyanine dyes, Reactive Blue 15 and Reactive Blue 38, were chosen as representatives of commercially used reactive dyes. From the 18 tested fungal strains only Bjerkandera adusta, Trametes versicolor and Phanerochaete chrysosporium were able to decolorize all the dyes tested. During degradation of the nickel-phthalocyanine complex, Reactive Blue 38, by B. adusta and T. versicolor respectively, the toxicity of this dye to Vibrio fischeri was significantly reduced. In the case of Reactive Violet 5, a far-reaching detoxification was achieved by treatment with B. adusta. Reactive Blue 38 and Reactive Violet 5 were decolorized by crude exoenzyme preparations from T. versicolor and B. adusta in a H2O2-dependent reaction. Specific activities of the exoenzyme preparations with the dyes were determined and compared to oxidation rates by commercial horseradish peroxidase.
Pascal Bonnarme - One of the best experts on this subject based on the ideXlab platform.
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Novel Scheme for Biosynthesis of Aryl Metabolites from L-Phenylalanine in the Fungus Bjerkandera adusta
Applied and environmental microbiology, 2000Co-Authors: Carmen Lapadatescu, Christian Ginies, Jean-luc Le Quéré, Pascal BonnarmeAbstract:Aryl metabolite biosynthesis was studied in the white rot fungus Bjerkandera adusta cultivated in a liquid medium supplemented with L-phenylalanine. Aromatic compounds were analyzed by gas chromatography-mass spectrometry following addition of labelled precursors ((14)C- and (13)C-labelled L-phenylalanine), which did not interfere with fungal metabolism. The major aromatic compounds identified were benzyl alcohol, benzaldehyde (bitter almond aroma), and benzoic acid. Hydroxy- and methoxybenzylic compounds (alcohols, aldehydes, and acids) were also found in fungal cultures. Intracellular enzymatic activities (phenylalanine ammonia lyase, aryl-alcohol oxidase, aryl-alcohol dehydrogenase, aryl-aldehyde dehydrogenase, lignin peroxidase) and extracellular enzymatic activities (aryl-alcohol oxidase, lignin peroxidase), as well as aromatic compounds, were detected in B. adusta cultures. Metabolite formation required de novo protein biosynthesis. Our results show that L-phenylalanine was deaminated to trans-cinnamic acid by a phenylalanine ammonia lyase and trans-cinnamic acid was in turn converted to aromatic acids (phenylpyruvic, phenylacetic, mandelic, and benzoylformic acids); benzaldehyde was a metabolic intermediate. These acids were transformed into benzaldehyde, benzyl alcohol, and benzoic acid. Our findings support the hypothesis that all of these compounds are intermediates in the biosynthetic pathway from L-phenylalanine to aryl metabolites. Additionally, trans-cinnamic acid can also be transformed via beta-oxidation to benzoic acid. This was confirmed by the presence of acetophenone as a beta-oxidation degradation intermediate. To our knowledge, this is the first time that a beta-oxidation sequence leading to benzoic acid synthesis has been found in a white rot fungus. A novel metabolic scheme for biosynthesis of aryl metabolites from L-phenylalanine is proposed.
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Production of aryl metabolites in solid-state fermentations of the white-rot fungus Bjerkandera adusta
Biotechnology Letters, 1999Co-Authors: Carmen Lapadatescu, Pascal BonnarmeAbstract:Bjerkandera adusta produced aromatic compounds such as benzaldehyde (bitter almond aroma), benzyl alcohol and benzoic acid from L-phenylalanine (3 g kg^−1). Two supports for the fungus, wheat bran (organic support) and Perlite (mineral support), gave optimal production with water contents of 66% and 60%, respectively. Benzyl alcohol (4.53 g kg^−1) and benzaldehyde (1.56 g kg^−1) were produced after 4 days on wheat bran respectively with 20 and 30 g L-phenylalanine kg^−1. Aryl alcohol oxidase activity, which oxidises benzyl alcohol to benzaldehyde, was only detected when the fungus was grown on wheat bran, the support which promotes the most benzaldehyde production. Results are compared with those obtained in submerged liquid cultures.
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Influence of cell immobilization on the production of benzaldehyde and benzyl alcohol by the white-rot fungi Bjerkandera adusta, Ischnoderma benzoinum and Dichomitus squalens
Applied Microbiology and Biotechnology, 1997Co-Authors: Carmen Lapadatescu, Gilles Feron, Catherine Vergoignan, A. Djian, A. Durand, Pascal BonnarmeAbstract:Three white-rot basidiomycetes, Bjerkandera adusta, Ischnoderma benzoinum and Dichomitus squalens, were cultivated on a liquid medium supplemented with l-phenylalanine, a precursor for benzaldehyde (bitter almond aroma) and benzyl alcohol. Remarkable amounts of benzaldehyde (587 mg l−1) were found in cultures of B. adusta. Immobilization of this fungus on polyurethane foam cubes allowed an 8.3-fold increase of the production of benzaldehyde and a 15-fold increase of the productivity as compared with non-immobilized cells. Aryl-alcohol oxidase activity was only detected in B. adusta. This activity was also significantly enhanced in immobilized cells, suggesting that it plays an important role in benzaldehyde biosynthesis. Conversely, consistent amounts of benzyl alcohol (340 mg l−1 for B. adusta and I. benzoinum and 100 mg l−1 for D. squalens) were produced by the three fungi when immobilized. Laccase activity was found only in the strains I. benzoinum and D. squalens. This activity was markedly enhanced in free cells cultures. Immobilization of the fungi did not promote benzyl alcohol production by comparison with free cell cultures (500 mg l−1).
Carmen Lapadatescu - One of the best experts on this subject based on the ideXlab platform.
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Novel Scheme for Biosynthesis of Aryl Metabolites from L-Phenylalanine in the Fungus Bjerkandera adusta
Applied and environmental microbiology, 2000Co-Authors: Carmen Lapadatescu, Christian Ginies, Jean-luc Le Quéré, Pascal BonnarmeAbstract:Aryl metabolite biosynthesis was studied in the white rot fungus Bjerkandera adusta cultivated in a liquid medium supplemented with L-phenylalanine. Aromatic compounds were analyzed by gas chromatography-mass spectrometry following addition of labelled precursors ((14)C- and (13)C-labelled L-phenylalanine), which did not interfere with fungal metabolism. The major aromatic compounds identified were benzyl alcohol, benzaldehyde (bitter almond aroma), and benzoic acid. Hydroxy- and methoxybenzylic compounds (alcohols, aldehydes, and acids) were also found in fungal cultures. Intracellular enzymatic activities (phenylalanine ammonia lyase, aryl-alcohol oxidase, aryl-alcohol dehydrogenase, aryl-aldehyde dehydrogenase, lignin peroxidase) and extracellular enzymatic activities (aryl-alcohol oxidase, lignin peroxidase), as well as aromatic compounds, were detected in B. adusta cultures. Metabolite formation required de novo protein biosynthesis. Our results show that L-phenylalanine was deaminated to trans-cinnamic acid by a phenylalanine ammonia lyase and trans-cinnamic acid was in turn converted to aromatic acids (phenylpyruvic, phenylacetic, mandelic, and benzoylformic acids); benzaldehyde was a metabolic intermediate. These acids were transformed into benzaldehyde, benzyl alcohol, and benzoic acid. Our findings support the hypothesis that all of these compounds are intermediates in the biosynthetic pathway from L-phenylalanine to aryl metabolites. Additionally, trans-cinnamic acid can also be transformed via beta-oxidation to benzoic acid. This was confirmed by the presence of acetophenone as a beta-oxidation degradation intermediate. To our knowledge, this is the first time that a beta-oxidation sequence leading to benzoic acid synthesis has been found in a white rot fungus. A novel metabolic scheme for biosynthesis of aryl metabolites from L-phenylalanine is proposed.
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Production of aryl metabolites in solid-state fermentations of the white-rot fungus Bjerkandera adusta
Biotechnology Letters, 1999Co-Authors: Carmen Lapadatescu, Pascal BonnarmeAbstract:Bjerkandera adusta produced aromatic compounds such as benzaldehyde (bitter almond aroma), benzyl alcohol and benzoic acid from L-phenylalanine (3 g kg^−1). Two supports for the fungus, wheat bran (organic support) and Perlite (mineral support), gave optimal production with water contents of 66% and 60%, respectively. Benzyl alcohol (4.53 g kg^−1) and benzaldehyde (1.56 g kg^−1) were produced after 4 days on wheat bran respectively with 20 and 30 g L-phenylalanine kg^−1. Aryl alcohol oxidase activity, which oxidises benzyl alcohol to benzaldehyde, was only detected when the fungus was grown on wheat bran, the support which promotes the most benzaldehyde production. Results are compared with those obtained in submerged liquid cultures.
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Influence of cell immobilization on the production of benzaldehyde and benzyl alcohol by the white-rot fungi Bjerkandera adusta, Ischnoderma benzoinum and Dichomitus squalens
Applied Microbiology and Biotechnology, 1997Co-Authors: Carmen Lapadatescu, Gilles Feron, Catherine Vergoignan, A. Djian, A. Durand, Pascal BonnarmeAbstract:Three white-rot basidiomycetes, Bjerkandera adusta, Ischnoderma benzoinum and Dichomitus squalens, were cultivated on a liquid medium supplemented with l-phenylalanine, a precursor for benzaldehyde (bitter almond aroma) and benzyl alcohol. Remarkable amounts of benzaldehyde (587 mg l−1) were found in cultures of B. adusta. Immobilization of this fungus on polyurethane foam cubes allowed an 8.3-fold increase of the production of benzaldehyde and a 15-fold increase of the productivity as compared with non-immobilized cells. Aryl-alcohol oxidase activity was only detected in B. adusta. This activity was also significantly enhanced in immobilized cells, suggesting that it plays an important role in benzaldehyde biosynthesis. Conversely, consistent amounts of benzyl alcohol (340 mg l−1 for B. adusta and I. benzoinum and 100 mg l−1 for D. squalens) were produced by the three fungi when immobilized. Laccase activity was found only in the strains I. benzoinum and D. squalens. This activity was markedly enhanced in free cells cultures. Immobilization of the fungi did not promote benzyl alcohol production by comparison with free cell cultures (500 mg l−1).
Nichina Gomi - One of the best experts on this subject based on the ideXlab platform.
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degradation of the synthetic dye amaranth by the fungus Bjerkandera adusta dec 1 inference of the degradation pathway from an analysis of decolorized products
Biodegradation, 2011Co-Authors: Nichina Gomi, Shuji Yoshida, Kazutsugu Matsumoto, Masayuki Okudomi, Hiroki Konno, Toru Hisabori, Yasushi SuganoAbstract:We examined the degradation of amaranth, a representative azo dye, by Bjerkandera adusta Dec 1. The degradation products were analyzed by high performance liquid chromatography (HPLC), visible absorbance, and electrospray ionization time-of-flight mass spectroscopy (ESI-TOF-MS). At the primary culture stage (3 days), the probable reaction intermediates were 1-aminonaphthalene-2,3,6-triol, 4-(hydroxyamino) naphthalene-1-ol, and 2-hydroxy-3-[2-(4-sulfophenyl) hydrazinyl] benzenesulfonic acid. After 10 days, the reaction products detected were 4-nitrophenol, phenol, 2-hydroxy-3-nitrobenzenesulfonic acid, 4-nitrobenzene sulfonic acid, and 3,4′-disulfonyl azo benzene, suggesting that no aromatic amines were created. Manganese-dependent peroxidase activity increased sharply after 3 days culture. Based on these results, we herein propose, for the first time, a degradation pathway for amaranth. Our results suggest that Dec 1 degrades amaranth via the combined activities of peroxidase and hydrolase and reductase action.
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degradation of the synthetic dye amaranth by the fungus Bjerkandera adusta dec 1 inference of the degradation pathway from an analysis of decolorized products
Biodegradation, 2011Co-Authors: Nichina Gomi, Shuji Yoshida, Kazutsugu Matsumoto, Masayuki Okudomi, Hiroki Konno, Toru Hisabori, Yasushi SuganoAbstract:We examined the degradation of amaranth, a representative azo dye, by Bjerkandera adusta Dec 1. The degradation products were analyzed by high performance liquid chromatography (HPLC), visible absorbance, and electrospray ionization time-of-flight mass spectroscopy (ESI-TOF-MS). At the primary culture stage (3 days), the probable reaction intermediates were 1-aminonaphthalene-2,3,6-triol, 4-(hydroxyamino) naphthalene-1-ol, and 2-hydroxy-3-[2-(4-sulfophenyl) hydrazinyl] benzenesulfonic acid. After 10 days, the reaction products detected were 4-nitrophenol, phenol, 2-hydroxy-3-nitrobenzenesulfonic acid, 4-nitrobenzene sulfonic acid, and 3,4′-disulfonyl azo benzene, suggesting that no aromatic amines were created. Manganese-dependent peroxidase activity increased sharply after 3 days culture. Based on these results, we herein propose, for the first time, a degradation pathway for amaranth. Our results suggest that Dec 1 degrades amaranth via the combined activities of peroxidase and hydrolase and reductase action.