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  • 1
    Electronic Resource
    Electronic Resource
    Removal of estrogenic activity of endocrine-disrupting genistein by ligninolytic enzymes from white rot fungi (2005)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 244 (2005), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Endocrine-disrupting genistein was treated with the white rot fungus Phanerochaete sordida YK-624 under ligninolytic condition with low-nitrogen and high-carbon culture medium. Genistein decreased by 93% after 4 days of treatment and the activities of ligninolytic enzymes, manganese peroxidase (MnP) and laccase, were detected during treatment, thus suggesting that the disappearance of genistein is related to ligninolytic enzymes produced extracellularly by white rot fungi. Therefore, genistein was treated with MnP, laccase, and the laccase-mediator system with 1-hydroxybenzotriazole (HBT) as a mediator. HPLC analysis demonstrated that genistein disappeared almost completely in the reaction mixture after 4 h of treatment with either MnP, laccase, or the laccase–HBT system. Using the yeast two-hybrid assay system, it was also confirmed that three enzymatic treatments completely removed the estrogenic activity of genistein after 4 h. These results strongly suggest that ligninolytic enzymes are effective in removing the estrogenic activity of genistein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/j.femsle.2005.01.023
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  • 2
    Electronic Resource
    Electronic Resource
    Lignin peroxidase is involved in the biobleaching of manganese-less oxygen-delignified hardwood kraft pulp by white-rot fungi in the solid-fermentation system (2004)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 233 (2004), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Biobleaching of manganese-less oxygen-delignified hardwood kraft pulp (E-OKP) by the white-rot fungi Phanerochaete sordida YK-624 and P. chrysosporium was examined in the solid-state fermentation system. P. sordida YK-624 possessed a higher brightening activity than P. chrysosporium, increasing pulp brightness by 13.4 points after seven days of treatment. In these fermentation systems, lignin peroxidase (LiP) activity was detected as the principle ligninolytic enzyme, and manganese peroxidase and laccase activities were scarcely detected over the course of treatment of E-OKP by either fungus. Moreover, a linear relationship between brightness increase and cumulative LiP activity was observed under all tested culture conditions with P. sordida YK-624 and P. chrysosporium. These results indicated that LiP is involved in the brightening of E-OKP by both white-rot fungi.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2004.tb09493.x
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  • 3
    Electronic Resource
    Electronic Resource
    Purification and characterization of a novel lignin peroxidase from white-rot fungus Phanerochaete sordida YK-624 (2003)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 224 (2003), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: We characterized kinetics and substrate oxidation of a novel lignin peroxidase (YK-LiP) isolated from white-rot fungus Phanerochaete sordida YK-624. YK-LiP enzyme was identified and purified to homogeneity by anion-exchange chromatography and gel permeation chromatography. The molecular mass of YK-LiP was approximately 50 kDa, and the absorption spectrum of YK-LiP was almost the same as that of the LiP (Pc-LiP) from Phanerochaete chrysosporium. Steady-state kinetics of veratryl alcohol oxidation by YK-LiP (unlike that by Pc-LiP) revealed a bi-reactant sequential mechanism, although reactivity of YK-LiP to various monomeric substituted aromatic compounds was similar to that of Pc-LiP. Degradation of dimeric lignin model compounds was more effective by YK-LiP than by Pc-LiP, and the oxidation rate of sinapyl alcohol oligomer by YK-LiP was much faster than that by Pc-LiP.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/S0378-1097(03)00447-6
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  • 4
    Electronic Resource
    Electronic Resource
    The metabolism of biphenyl structures in lignin by the wood-rotting fungus Coriolus versicolor (1989)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 61 (1989), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract In the degradation of lignin by the wood-rotting fungus Coriolus versicolor, understanding the metabolism of biphenyl structure is one of the most important steps in elucidation of the depolymerization process. This study gave the first evidence of aromatic ring fission of a biphenyl structure type by C. versicolor. The degradation of biphenyl structures of lignin by this fungus occurred to a slight extent as a result of a non-specific system. This phenomenon was observed only in a medium in which phenol oxidase was actively produced by this fungus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1989.tb03642.x
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  • 5
    Electronic Resource
    Electronic Resource
    Characteristics of novel lignin peroxidases produced by white-rot fungus Phanerochaete sordida YK-624 (2005)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 246 (2005), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: We characterized a lignin peroxidase (YK-LiP2) isolated from shaking culture inoculated with the white-rot fungus Phanerochaete sordida YK-624. The YK-LiP2 enzyme was identified and purified to homogeneity by anion-exchange chromatography and gel permeation chromatography. The molecular weight of YK-LiP2 was approximately 45 kDa, and its absorption spectrum was almost the same as that of the LiP (Pc-LiP) from P. chrysosporium. Steady-state kinetics of veratryl alcohol (VA) oxidation by YK-LiP2 revealed an ordered bi-bi ping-pong mechanism, although the Pc-LiP oxidation of ferrocytochrome c obeys peroxidase ping-pong kinetics rather than ordered bi-bi ping-pong kinetics. Degradation of dimeric lignin model compounds by YK-LiP2 was more effective than that by Pc-LiP. Moreover, YK-LiP2 and YK-LiP1, which was previously isolated from static culture inoculated with P. sordida YK-624, oxidized VA under a higher concentration of hydrogen peroxide (〉2.5 mM) although Pc-LiP could not oxidize VA in the presence of 2.5 mM hydrogen peroxide.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/j.femsle.2005.03.032
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  • 6
    Electronic Resource
    Electronic Resource
    Polyethylene degradation by lignin-degrading fungi and manganese peroxidase (1998)
    Springer
    Journal of wood science 44 (1998), S. 222-229 
    Details
    ISSN: 1611-4663
    Keywords: Polyethylene ; Biodegradation ; Lignindegrading fungi ; Manganese peroxidase ; Ligninolytic activity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Abstract Degradation of high-molecular-weight polyethylene membrane by lignin-degrading fungi, IZU-154, Phanerochaete chrysosporium, and Trametes versicolor, was investigated under various nutritional conditions. IZU-154 showed the most significant polyethylene degradation among the three lignin-degrading fungi under nitrogen- or carbon-limited culture conditions. Furthermore, for T. versicolor and P. chrysosporium, the addition of Mn(II) into nitrogen- or carbon-limited culture medium enhanced polyethylene degradation. These results suggest that polyethylene degradation is related to ligninolytic activity of lignin-degrading fungi. Treatment of polyethylene membrane with partially purified manganese peroxidase (MnP) caused significant degradation in the presence of Tween 80, Mn(II), and Mn(III) chelator. This result demonstrates that MnP is the key enzyme in polyethylene degradation by lignin-degrading fungi.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00521967
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  • 7
    Electronic Resource
    Electronic Resource
    Structural changes of residual lignin in softwood kraft pulp treated with manganese peroxidase (1998)
    Springer
    Journal of wood science 44 (1998), S. 327-331 
    Details
    ISSN: 1611-4663
    Keywords: Kraft pulp ; Residual lignin ; Manganese peroxidase ; Functional group ; Alkaline nitrobenzene oxidation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Abstract Structural changes of residual lignin in unbleached softwood kraft pulp (SWKP) during manganese peroxidase (MnP) treatment were investigated to obtain some understanding of the biobleaching action of SWKP with MnP treatment. Alkaline-extracted lignin from darkened SWKP by MnP showed more intense color and contained moreo-quinone than that from control SWKP. However, no difference in the conjugatedα-carbonyl was observed between the lignins from MnP-treated and control SWKP. The nitrobenzene oxidation analysis revealed that oxidative condensation of non-condensed lignin in SWKP occurs during an early stage of MnP treatment. These observations were supported by the model experiment in which the lignin prepared from control SWKP was subjected to MnP treatments three times, and the changes of color and functional groups in the lignin were determined after each treatment. These results suggested that an increase ino-quinone and the condensation reaction of non-condensed lignin in SWKP are responsible for the characteristic darkening of SWKP during MnP treatment. It was also ascertained that darkened lignin was degraded and brightened by repeated MnP treatments.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00581315
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  • 8
    Electronic Resource
    Electronic Resource
    In vitro screening of angiotensin I-converting enzyme inhibitors from Japanese cedar (Cryptomeria japonica) (1998)
    Springer
    Journal of wood science 44 (1998), S. 463-468 
    Details
    ISSN: 1611-4663
    Keywords: ACE inhibitor ; Cryptomeria japonica ; Catechin ; Procyanidin B3 ; Flavonoid
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Abstract Screening and isolation of angiotensin I-converting enzyme (ACE) inhibitors from Japanese cedar (Cryptomeria japonica) based on the in vitro ACE inhibitory assay were attempted. The ethanol extract from outer bark showed the highest inhibitory activity (IC50 is 16μg/ml) among 24 extracts prepared from roots, leaves, heartwood, sapwood, inner bark, and outer bark by successive extraction with four solvents. The fractionation of the outer bark ethanol extract followed by the bioassay resulted in the isolation of two strong ACE inhibitors, catechin and dimeric procyanidin B3. The bioassay of three flavan-3-ols including (+)-catechin and six flavones revealed that most of these compounds have high ACE inhibitory activity. The results suggest that the phenolic hydroxyl group at the C7 position and heterocyclic oxygen atom of these compounds are important for expressing the inhibitory activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00833411
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  • 9
    Electronic Resource
    Electronic Resource
    Role of Tween 80 in biobleaching of unbleached hardwood kraft pulp with manganese peroxidase (2000)
    Springer
    Journal of wood science 46 (2000), S. 137-142 
    Details
    ISSN: 1611-4663
    Keywords: Lignin ; Manganese peroxidase ; Biobleaching ; Surfactant ; Lipid peroxidation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Abstract The role of Tween 80 in biobleaching of unbleached hardwood kraft pulp (HWKP) with manganese peroxidase (MnP) was investigated. Among the surfactants (e.g., Tween 80, Tween 20, CHAPSO) the most significant brightness increase was obtained with Tween 80. Tween 80 and Tween 20 exhibited several effects, such as dispersion of degraded lignin and activation of MnP, that partly contributed to the brightening of HWKP during MnP treatment. However, these characteristics did not explain the most appreciable effect on the brightness increase by Tween 80. Lipid peroxidation of surfactants during MnP biobleaching was determined by measuring the peroxide value (POV). The order of the POV increase was consistent with that of the brightness increase of pulp during MnP treatment in the presence of various surfactants or linolenic acid. However, radicals and peroxides derived from lipid (linolenic acid) peroxidation by lipoxidase hardly brightened the HWKP by themselves. These results suggested that Tween 80 was peroxidized by Mn(III), and that Mn(III) and lipid peroxidation of Tween 80 synergistically brightened HWKP.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00777360
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  • 10
    Electronic Resource
    Electronic Resource
    Polyethylene degradation by manganese peroxidase in the absence of hydrogen peroxide (2000)
    Springer
    Journal of wood science 46 (2000), S. 180-183 
    Details
    ISSN: 1611-4663
    Keywords: Polyethylene ; Biodegradation ; Manganese peroxidase ; Surfactant
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Abstract A possible role of Tween 80 in the polyethylene degradation by manganese peroxidase (MnP) and the basis of the MnP action in the absence of hydrogen peroxide were investigated. The MnP activity in the system was retained its maximum level for 6 days in the presence of Tween 80. Tween 20 and CHAPSO stabilized MnP in the system similarly to Tween 80, and these surfactants also promote the polyethylene degradation. The system containing malonate buffer, Mn(II), and MnP produced Mn(III) in the absence of hydrogen peroxide, but the effect of Tween 80 addition on Mn(III) production in the absence of hydrogen peroxide was small. The results show that Mn(III) is generated by the MnP action initiated and amplified by the decomposition of malonate by Mn(III) and that a surfactant such as Tween 80 is required to stabilize MnP in the system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00777369
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