Effects of melecular oxygen on lignin degradation by Phanerochaete chrysosporium

Bar-lev, S.; Kirk, T. Kent

doi:10.1016/0006-291x(81)91755-1

Cited by 123 publications

(47 citation statements)

References 8 publications

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“…P. chrysosporium strain BKM-F-1767 (= ATCC 24725) was grown at 39°C in shallow stationary cultures as previously described (24), except that 0.01 M trans-aconitic acid (pH 4.3) was used as the growth buffer instead of 2,2-dimethylsuccinic acid. The stoppered cultures were flushed with 100% 02 after 2 Enzyme assays. H202-producing activity was determined by using a modified peroxidase-coupled assay with phenol red as the peroxidase substrate (36).…”

Section: Methodsmentioning

confidence: 99%

“…The ligninolytic system of this organism is expressed in defined media in response to nutrient carbon, nitrogen, or sulfur limitation (19,23,25,38). Other factors, such as 02 partial pressure, agitation, metal ion balance, and pH, are also important (2,19,25,30). Under ligninolytic conditions, P. chrysosporium produces extracellular H202 (10) and a number of H202-requiring peroxidases (ligninases) that oxidize and partially depolymerize lignin or lignin model compounds (14,31,39,41,42).…”

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confidence: 99%

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Involvement of a new enzyme, glyoxal oxidase, in extracellular H2O2 production by Phanerochaete chrysosporium

Kersten¹,

Kirk²

1987

J Bacteriol

338

213

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The importance of extracellular H202 in lignin degradation has become increasingly apparent with the recent discovery of H202-requiring ligninases produced by white-rot fungi. Here we describe a new H202-producing activity of Phanerochaete chrysosporium that involves extraceliular oxidases able to use simple aldehyde, a-hydroxycarbonyl, or a-dicarbonyl compounds as substrates. The activity is expressed during secondary metabolism, when the ligninases are also expressed. Analytical isoelectric focusing of the extracellular proteins, followed by activity staining, indicated that minor proteins with broad substrate specificities are responsible for the oxidase activity. Two of the oxidase substrates, glyoxal and methylglyoxal, were also identified, as their quinoxaline derivatives, in the culture fluid as secondary metabolites. The significance of these findings is discussed with respect to lignin degradation and other proposed systems for H202 production in P. chrysosporium.The white-rot wood-metabolizing basidiomycetes appear to be major degraders of lignin, and, of these, Phanerochaete chrysosporium is the most widely studied species. The ligninolytic system of this organism is expressed in defined media in response to nutrient carbon, nitrogen, or sulfur limitation (19,23,25,38). Other factors, such as 02 partial pressure, agitation, metal ion balance, and pH, are also important (2,19,25,30). Under ligninolytic conditions, P. chrysosporium produces extracellular H202 (10) and a number of H202-requiring peroxidases (ligninases) that oxidize and partially depolymerize lignin or lignin model compounds (14,31,39,41,42).Several schemes have been proposed for the production of extracellular H202 in ligninolytic cultures. These involve either intracellular enzymes, including glucose-l-oxidase (20), glucose-2-oxidase (9), and fatty acyl-coenzyme A oxidase (16), or extracellular Mn2+-dependent peroxidases that reduce 02 to H202 by using NADH, NADPH, or glutathione as an electron source (1,13,34,35).Here we describe a new H202-producing activity, which we term glyoxal oxidase, from P. chrysosporium. Importantly, this activity, as well as two of its many substrates, glyoxal and methylglyoxal, are found in the extracellular fluid of ligninolytic cultures. Extracellular production of H202 seems particularly relevant to the lignin biodegradation process because the ligninases are extracellular and the organism has strong intracellular catalase activity (15). MATERIALS AND METHODSOrganism and culture conditions. P. chrysosporium strain BKM-F-1767 (= ATCC 24725) was grown at 39°C in shallow stationary cultures as previously described (24) Enzyme assays. H202-producing activity was determined by using a modified peroxidase-coupled assay with phenol red as the peroxidase substrate (36). The reaction mixture contained 50 mM Na+ 2,2-dimethylsuccinate (pH 6.0), 10 mM oxidase substrate, 0.01% phenol red, 10 ,ug of horseradish peroxidase (type II; Sigma Chemical Co., St. Louis, Mo.), and up to 300 RI of culture fluid in a total react...

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Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

Involvement of a new enzyme, glyoxal oxidase, in extracellular H2O2 production by Phanerochaete chrysosporium

Kersten¹,

Kirk²

1987

J Bacteriol

338

213

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“…By contrast, in liquid cultures (suitable for industrial fermentation) the fungal spore inoculum develops into mycelial pellets, which are agglomerates of hyphae trapped together during germination of the spores (Gerin et al, 1993). The pellet habit represents a significant obstacle to oxygen diffusion into the hyphae (Leisola et al, 1983 ;Michel et al, 1992) Bar-Lev & Kirk, 1981 ;Faison & Kirk, 1985). The role of oxygen has been ascribed to either its direct participation in ligninolysis (Kirk et al, 1978) or its capacity to promote the synthesis of one or more enzymes involved in lignin degradation (Bar-Lev & Kirk, 1981).…”

Section: Abbreviationsmentioning

confidence: 99%

“…The pellet habit represents a significant obstacle to oxygen diffusion into the hyphae (Leisola et al, 1983 ;Michel et al, 1992) Bar-Lev & Kirk, 1981 ;Faison & Kirk, 1985). The role of oxygen has been ascribed to either its direct participation in ligninolysis (Kirk et al, 1978) or its capacity to promote the synthesis of one or more enzymes involved in lignin degradation (Bar-Lev & Kirk, 1981). Alternatively, the necessity to expose fungal pellets or mats in liquid culture to a pure oxygen atmosphere has been ascribed to the need to ameliorate conditions of oxygen starvation (Leisola et al, 1983 ;Michel et al, 1992).…”

Section: Abbreviationsmentioning

confidence: 99%

“…Alternatively, the necessity to expose fungal pellets or mats in liquid culture to a pure oxygen atmosphere has been ascribed to the need to ameliorate conditions of oxygen starvation (Leisola et al, 1983 ;Michel et al, 1992). To overcome the oxygen limitation to LiP production, a practice has evolved that involves exposing hyphal pellets to an atmosphere of pure oxygen when the culture medium has been depleted of carbon (supplied as glucose), nitrogen or sulphur (Kirk et al, 1978 ;Bar-Lev & Kirk, 1981 ;Leisola & Fiechter, 1985 ;Faison & Kirk, 1985 ;Jager et al, 1985 ;Asther et al, 1987 ;Michel et al, 1990 ;Dosoretz et al, 1990 ;Dass & Reddy, 1990 ;Bonnarme et al, 1993).…”

Section: Abbreviationsmentioning

confidence: 99%

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Disordered ultrastructure in lignin-peroxidase-secreting hyphae of the white-rot fungus Phanerochaete chrysosporium

2000

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The practice of exposing liquid cultures of the white-rot fungus Phanerochaete chrysosporium to a pure oxygen atmosphere under conditions of nutrient starvation has been widely adopted to induce lignin peroxidase (LiP) synthesis. Transmission electron microscopy was used to examine hyphal cells of carbonlimited cultures that had been exposed to an atmosphere of pure oxygen, and revealed evidence of a major loss in organization of cellular ultrastructure, which may be attributed to oxygen toxicity. Under some conditions (continuous agitation in air with cellulose as the carbon source) cultures will produce LiP without needing to be exposed to a pure oxygen atmosphere. A similar major loss of cellular ultrastructure was found in hyphal cells from such cultures upon examination. Investigation of the levels of H 2 O 2 , catalase and carbonyl content of intracellular proteins suggests that the latter cultures developed a hyperoxidant state because the rate of supply of carbon from cellulose hydrolysis was insufficient for oxygen homeostasis. The association of LiP with these cultures and with those exposed to an atmosphere of pure oxygen infers that LiP may be triggered in response to oxidant stress.

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Degradation of lignocellulosic residues by polyporus versicolor and the effect of moisture contents and phenolic compounds

Arora

Sandhu

1986

Acta Biotechnologica

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Polyporus versicolor was selected to find out its ability to degrade four different lignocellulosic residues (angiospermic wood sawdust, sugarcane bagasse, paddy and wheat straw) under semisolid conditions. The production of laccase was also studied on these substrates. Sawdust suffered a maximum lignin loss though overall reduction in weight was maximum in paddy straw. Addition of malt extract and certain phenolic compounds (gallic acid, tannic acid and orcinol) favoured ligninolysis in sawdust. A moisture level of 5 ml/g of sawdust was found to be the most suitable for degradation whereas laccase yield increased with further rise in moisture content.

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Effects of melecular oxygen on lignin degradation by Phanerochaete chrysosporium

Cited by 123 publications

References 8 publications

Involvement of a new enzyme, glyoxal oxidase, in extracellular H2O2 production by Phanerochaete chrysosporium

Involvement of a new enzyme, glyoxal oxidase, in extracellular H2O2 production by Phanerochaete chrysosporium

Disordered ultrastructure in lignin-peroxidase-secreting hyphae of the white-rot fungus Phanerochaete chrysosporium

Degradation of lignocellulosic residues by polyporus versicolor and the effect of moisture contents and phenolic compounds

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