Dactyliumdendroides (Bull.) Fr. Misnamed as Polyporuscircinatus Fr

Nobles, Mildred K.; Madhosingh, C.

doi:10.1016/0006-291x(63)90251-1

Cited by 30 publications

(17 citation statements)

References 3 publications

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“…(Note that Dactylium dendroides, a deuteromycete, has been misnamed as Polyporus circinatus in related studies [33], and therefore the source of the galactose oxidase was possibly D. dendroides.)…”

Section: Resultsmentioning

confidence: 99%

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

Kersten¹,

Kirk²

1987

J Bacteriol

337

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: Resultsmentioning

confidence: 99%

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

Kersten¹,

Kirk²

1987

J Bacteriol

337

213

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“…The kinetics, chemistry and oxidative mechanism of GAO have been thoroughly studied (reviewed in [4,5]). Briefly, the catalytic reaction of GAO comprises oxidative and reductive halfreactions, using molecular oxygen as an electron acceptor and producing hydrogen peroxide.…”

Section: Galactose Oxidasementioning

confidence: 99%

“…The mechanism and kinetics of GAO-catalyzed oxidation have been previously extensively studied and reviewed [4][5]. Accordingly, this review focuses on a new perspective: the utilization of GAO in synthetic applications, such as the modification of galactose-containing mono-, oligoand polysaccharides.…”

Section: Introductionmentioning

confidence: 99%

Oxidation with galactose oxidase: Multifunctional enzymatic catalysis

Parikka

Master

Tenkanen

2015

Journal of Molecular Catalysis B: Enzymatic

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“…The production of extra cellular GO has been detected in a few species of filamentous fungi, including Fusarium graminearum (Avigad et al, 1962;Tressel and Kosman, 1982;Barbosa-Tessmann et al, 2001), Gibberella fujikuroi (Aisaka and Terada, 1981), and F. acuminatum (Barbosa-Tessmann et al, 2001). The majority of the studies with GO have been done with F. graminearum (NRRL 2903; ATCC 46032), isolated as a mycoparasite of the basidiomicete Polyporus circinatus, and initially identified as Dactylium dendroides in Southern Brazil (Avigad et al, 1962;Nobles and Madhosingh, 1963;Ögel et al, 1994;Niessen and Vogel, 1997). This isolate has been used for the industrial production of GO.…”

Section: Introductionmentioning

confidence: 99%

Production and characterization of galactose oxidase produced by four isolates of Fusarium graminearum

Gasparotto

Abrão

Inagaki

et al. 2006

Braz. arch. biol. technol.

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A screening aimed to find new galactose oxidase producer isolates and to evaluate the production among Fusarium graminearum strains was conducted. Thirty-five isolates out of 39 analysed produced the enzyme at several levels. The data indicated a wide distribution of galactose oxidase within F. graminearum and also revealed new producer isolates. The enzyme produced by different isolates showed similar thermal activity and stability and were active on same substrates. However, the optimum pH ranged from 7.0 to 7.5. Thus, all evaluated isolates were suitable for the production of galactose oxidase.

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Dactyliumdendroides (Bull.) Fr. Misnamed as Polyporuscircinatus Fr

Cited by 30 publications

References 3 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

Oxidation with galactose oxidase: Multifunctional enzymatic catalysis

Production and characterization of galactose oxidase produced by four isolates of Fusarium graminearum

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