Evidence for a new extracellular peroxidase Manganese‐inhibited peroxidase from the white‐rot fungus <i>Bjerkandera</i> sp. BOS 55

Jong, Ed de; Field, Jim A.; Bont, J.A.M. de

doi:10.1016/0014-5793(92)80111-s

Cited by 75 publications

(38 citation statements)

References 18 publications

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“…Moreover, the Mn2+-independent peroxidase activity of P. eryngii MP at pH 5 is more significant at relatively high concentrations of 2,6-dimethoxyphenol, attaining 50% activity (with respect to that found in presence of Mn2+) when the 2,6-dimethoxyphenol concentration is 0.5 mM. A manganese-independent peroxidase (MIP), first described as Mn'+-inhibited peroxidase, has been reported in B. adusta [54], although it has not been fully characterized.…”

Section: Discussionmentioning

confidence: 98%

Purification and Catalytic Properties of Two Manganese Peroxidase Isoenzymes from Pleurotus eryngii

Martı́nez

Ruíz-Dueñas

Guillén

et al. 1996

European Journal of Biochemistry

341

244

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The ligninolytic basidiomycetes Pleurotus eryngii, Pleurotus ostreatus, Pleurotus pulmonarius and Pleurotus sajor-caju did not exhibit detectable levels of manganese peroxidase (MP) when grown in liquid media with ammonium tartrate as N source. However, after examination of cells grown on different organic N-based media, high M P activity was obtained in peptone medium, up to nearly 3 U/ml in cultures of I? eryngii. Moreover, Mnz+ supplementation was not used to produce MP, since all Mn2+ concentrations assayed (1 -4000 pM) inhibited production of this enzyme in liquid medium.Two MP isoenzymes were purified to homogeneity from shaken or stationary cultures of I? eryngii grown in peptone medium. The purification process (which included chromatography on Biorad Q-cartridge, Sephacryl S-200 and Mono-Q) attained 56% activity yield with a purification factor of 25. The isoenzymes differed in PI (3.75 and 3.65), N-terminal sequence and some catalytic properties. They were in some aspects (e.g., molecular mass of 43 kDa) similar to Phanerochaete chrysosporium MP but exhibited some distinct characteristics, including Mn"-independent peroxidase activities against 2,6-dimethoxyphenol and veratryl alcohol, and higher resistance to H,O,. Recent studies have shown that M P are ubiquitous enzymes in ligninolytic fungi, but the results obtained suggest that differences in catalytic properties probably exist between different Mn2 ' -oxidizing peroxidases produced by these fungi.

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Section: Discussionmentioning

confidence: 98%

Purification and Catalytic Properties of Two Manganese Peroxidase Isoenzymes from Pleurotus eryngii

Martı́nez

Ruíz-Dueñas

Guillén

et al. 1996

European Journal of Biochemistry

341

244

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“…The Syringaldazine well test indicated the secretion of laccase by P. pulmonarius and P. sajor-caju as observed by the appearance of purple color around each well (Figure 2e) whereas the faint pink colour in S. commune suggests enhanced levels of LiP and MnP than laccase. Similarly, Devi et al (2012) Jong et al (1992) also reported that 18 fungi out of 20 screened produced MnP and laccase but their decolourization rate varied based on the substrate used. Like in our study, Swamy and Ramsay (1999) reported that in the white rot fungus, T. versicolor produced laccase and manganese peroxidase (MnP) that could decolorize the amaranth azo dye.…”

Section: Screening Of White Rot Fungi For Lignolytic Enzymesmentioning

confidence: 93%

Extracellular secretion of lignocellulolytic enzymes by diversewhite rot asidiomycetes fungi

Thiribhuvanamala¹,

Kalaiselvi²,

Parthasarathy³

et al. 2017

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Rich source of biota includes several white rot fungi, were reported in Western Ghats regions of Tamil Nadu, India. The effective identification of white rot fungi and their lignocellulolytic enzymes play a crucial role for degradation of agricultural and industrial wastes to maintain su sta ina ble ecosystem. T hus, the present study was conducted to assess the secretion of lignocellulolytic enzymes of diverse white rot fungi, collected from Western Ghats regions of Tamil Nadu, comprising of Kotagiri and Ooty of the Nilgiri district, Siruvani and Anaikati of Coimbatore district. A total of 16 white rot fungi belonging to 6 genera, viz., Pleurotus spp., Lentinus spp., Ganoderma spp., Trametes spp., Pycnoporus spp. and Schizophyllum spp. were collected and identified through morphological and molecular methods. The activity of cellulase enzyme was prominently visible in Pleurotus pulmonarius, P. sajar-caju, Pycnoporus sanguineus, P. ostreatus, Ganoderma gibbosum and Schizophyllum commune and hemicellulolytic activity was maximum in Trametes ijubarskii, Lentinus crinitus, P. sanguineus and G. gibbosum . The quantitative and qualitative screening for major lignolytic enzymes, viz., laccase (Lac), lignin peroxidase (LiP) and manganese peroxidase (MnP) revealed significant levels of Lac secretion when compared to LiP and MnP by P. pulmonarius, P. sajar-caju and Schizophyllum commune. The syringaldazine well test further confirmed the secretion of laccase as major enzyme followed by LiP and MnP. Also the Lac and LiP activity was maximum at pH of 4.5 and MnP activity at pH of 5.0 by P. pulmonarius, P. sajar caju and S. commune. Temperature of 30°C induced maximum secretion of Lac, LiP and MnP by these three fungi. A significant level of Lac was observed on 4 th day after inoculation while LiP and MnP was maximum on 7 th and 8 th day for P. pulmonarius and P. sajar-caju. Whereas, S. commune secreted significant levels of Lac on 10 th to 11 th da y, while LiP and MnP on 6 th and 7 th da y. This study paves the way for u se of P. pulmonarius, P. sajar-caju and S. commune for biodegradation and bioconversion of agrowastes.

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“…These fungi are the only organisms with a demonstrated capacity to both depolymerize and mineralize lignin by an oxidative and nonspecific mechanism (30). Besides laccase, the ligninolytic system of these fungi includes several peroxidases (9,16,36,48), known as lignin peroxidase and manganese peroxidase (MnP), and oxidases that produce the hydrogen peroxide (H 2 O 2 ) needed for peroxidase activities (18,29). Another enzyme produced by these fungi, which functions in the degradation of not only lignin but also cellulose, is cellobiose dehydrogenase (11).…”

mentioning

confidence: 99%

Oxygen Activation during Oxidation of Methoxyhydroquinones by Laccase from Pleurotus eryngii

Guillén

Muñoz

Gómez-Toribio

et al. 2000

Appl Environ Microbiol

105

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Oxygen activation during oxidation of the lignin-derived hydroquinones 2-methoxy-1,4-benzohydroquinone (MBQH 2 ) and 2,6-dimethoxy-1,4-benzohydroquinone (DBQH 2 ) by laccase from Pleurotus eryngii was examined. Laccase oxidized DBQH 2 more efficiently than it oxidized MBQH 2 ; both the affinity and maximal velocity of oxidation were higher for DBQH 2 than for MBQH 2 . Autoxidation of the semiquinones produced by laccase led to the activation of oxygen, producing superoxide anion radicals (

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Evidence for a new extracellular peroxidase Manganese‐inhibited peroxidase from the white‐rot fungus Bjerkandera sp. BOS 55

Cited by 75 publications

References 18 publications

Purification and Catalytic Properties of Two Manganese Peroxidase Isoenzymes from Pleurotus eryngii

Purification and Catalytic Properties of Two Manganese Peroxidase Isoenzymes from Pleurotus eryngii

Extracellular secretion of lignocellulolytic enzymes by diversewhite rot asidiomycetes fungi

Oxygen Activation during Oxidation of Methoxyhydroquinones by Laccase from Pleurotus eryngii

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