[19] Galactose oxidase of Polyporus circinatus1–4

Amaral, D.; Kelly-Falcoz, Francoise; Horecker, B.L.

doi:10.1016/0076-6879(66)09023-2

Cited by 75 publications

(53 citation statements)

References 11 publications

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“…In contrast, the lack of activity of the enzymes on glucose indicated that the stereo configuration of the OH-group at the carbon-4 was important for their activities. The results for the GO from the GOPS were in agreement with the reports in the literature (Whittaker, 2003;Wittaker, 2002;Mazur, 1991;Chiu et al, 1996;Sun et al, 2001;Amaral et al, 1966;Cooper et al, 1958;Avigad et al, 1962;Ettinger and Kosman, 1981). The optimum pH, temperature, thermal stability, and substrate specificity for the enzyme of the four tested isolates were similar when compared with the GO from GOPS.…”

Section: Resultssupporting

confidence: 82%

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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Section: Resultssupporting

confidence: 82%

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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“…GO activity was assayed by the peroxidase/o-dianisidine colorimetric method (3,28), based on the estimation of the colored oxidized o-dianisidine. Filtrate (0.5 ml pure or diluted); 1.4 ml of the reactive mixture [50 mM phosphate buffer, pH 7.0; 0.2 mg/ml o-dianisidina (Sigma D-3252; previously dissolved in methanol 2 mg/ml); 0.04 mg/ml (6.0 U/ml) peroxidase (Sigma P-8125)]; and 0.1 ml of 0.5 M D-(+)-galactose were mixed and incubated for 10 minutes at 30ºC.…”

Section: Enzyme Assaymentioning

confidence: 99%

“…Extra cellular production of GO has been shown for F. graminearum (3,5,7), Gibberella fujikuroi (2), Fusarium moniliforme f. sp. subglutinans (5), and Fusarium acuminatum (5).…”

Section: Introductionmentioning

confidence: 99%

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A new PCR approach for the identification of Fusarium graminearum

Biazio¹,

Leite²,

Tessmann³

et al. 2008

Braz. J. Microbiol.

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The main objective of this work was to develop a PCR protocol for the identification of Fusarium graminearum, based on a pair of primers targeted to a segment of the 3´coding region of the gaoA gene that codes for the enzyme galactose oxidase (GO). This region has low homology with the same region of GO genes from other fungi. Genomic DNA from 17 strains of Fusarium spp. isolated from diseased cereals, from several other Fusarium species, and from other fungi genera was analyzed in a PCR assay using this primer set. The 17 strains of Fusarium spp. were also analyzed for the GO enzyme production in submerse fermentation in a new formulated liquid medium. All strains that were morphologically and molecularly identified as F. graminearum were able to secrete the enzyme and had a positive result in the used PCR protocol. No DNA fragment was amplified using genomic DNA from other Fusarium species and species of other fungi genera. The results suggest that the proposed PCR protocol is specific and can be considered as a new molecular tool for the identification of F. graminearum. In addition, the new formulated medium is a cheap alternative for screening for GO screening production by F. graminearum.

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“…This enzyme catalyses oxidation of D-galactose to galactohexodialdose, which reduces molecular oxygen to hydrogen peroxide, and has been used for the specific determination of D-galactose (2).…”

Section: Introductionmentioning

confidence: 99%

Production of mycotoxins by galactose oxidase producing Fusarium using different culture

Pereira

Kemmelmeier

2000

Braz. J. Microbiol.

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The original isolate of the galactose oxidase producing fungus Dactylium dendroides, and other five galactose oxidase producing Fusarium isolates were cultivated in different media and conditions, in order to evaluate the production of 11 mycotoxins, which are characteristic of the genus Fusarium: moniliformin, fusaric acid, deoxynivalenol, fusarenone-X, nivalenol, 3-acetyldeoxynivalenol, neosolaniol, zearalenol, zearalenone, acetyl T-2, and iso T-2. The toxicity of the culture extracts to Artemia salina larvae was tested.

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[19] Galactose oxidase of Polyporus circinatus1–4

Cited by 75 publications

References 11 publications

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

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

A new PCR approach for the identification of Fusarium graminearum

Production of mycotoxins by galactose oxidase producing Fusarium using different culture

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