Isolation, purification and characterization of a novel glucose oxidase from Penicillium sp. CBS 120262 optimally active at neutral pH

Simpson, C.F.; Jordaan, Justin; Gardiner, N.S.; Whiteley, Chris G.

doi:10.1016/j.pep.2006.09.013

Cited by 37 publications

(33 citation statements)

References 20 publications

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“…The calculated K M values for invertase and GO lie within the ranges mentioned in the literature, i.e., 26-40 mM (Milovanovic et al, 2007;Dizge et al, 2008) and 18-32 mM (Simpson et al, 2007;Hoshi et al, 2007), respectively.…”

Section: Resultssupporting

confidence: 80%

“…Under these conditions, it could be speculated that both enzymes do not suffer modification in their respective molecular structures. According to the literature, invertase may have kept its molecules aggregated (De Queiroz et al, 1996), whereas GO kept its prosthetic groups Fe +2 /Fe +3 and FAD/FADH 2 in the reduced and oxidized forms, respectively (Tomotani, 2006;Simpson et al, 2007;Bao et al, 2001). Consequently, conversion of sucrose into fructose and gluconic acid in a continuous multi enzymatic membrane reactor for 15 h, would most likely occur with the main enzymes (GO and invertase) in their ideal molecular conformation.…”

Section: Resultsmentioning

confidence: 99%

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Invertase, glucose oxidase and catalase for converting sucrose to fructose and gluconic acid through batch and membrane-continuous reactors

Silva

Tomotani

Vítolo

2011

Braz. J. Pharm. Sci.

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Conversion of sucrose into fructose and gluconic acid using invertase, glucose oxidase and catalase was studied by discontinuous (sequential or simultaneous addition of the enzymes) and continuous (simultaneous addition of the enzymes in a 100 kDa-ultrafiltration membrane reactor) processes. The following parameters were varied: concentration of enzymes, initial concentration of substrates (sucrose and glucose), pH, temperature and feeding rate (for continuous process). The highest yield of conversion (100%) was attained through the discontinuous (batch) process carried out at pH 4.5 and 37 ºC by the sequential addition of invertase (14.3 U), glucose oxidase (10,000 U) and catalase (59,000 U).
Neste trabalho estudou-se a conversão da sacarose em frutose e ácido glicônico, usando as enzimas invertase, glicose oxidase e catalase, através do emprego de processo descontínuo (com adição sequencial ou simultânea das enzimas) e contínuo (adição simultânea das enzimas em reator com membrana acoplado à membrana de ultrafiltração de 100 kDa). Os parâmetros variados foram: a concentração das enzimas, a concentração inicial dos substratos (sacarose e glicose), o pH, a temperatura e a vazão específica de alimentação (processo contínuo). Obteve-se rendimento de 100%, quando a conversão foi conduzida por processo descontínuo em pH 4,5 e a 37 ºC com adição seqüencial das enzimas invertase (14,3 U), glicose oxidase (10.000 U) e catalase (59.000 U)

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Section: Resultssupporting

confidence: 80%

Section: Resultsmentioning

confidence: 99%

Invertase, glucose oxidase and catalase for converting sucrose to fructose and gluconic acid through batch and membrane-continuous reactors

Silva

Tomotani

Vítolo

2011

Braz. J. Pharm. Sci.

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“…GOx is mostly found in fungal strains, such as genus Aspergillus (Hatzinikolaou et al, 1996), Penicillium (Simpson et al, 2007), Saccharomyces cerevisiae (Zakhartsev and Momeu, 2007) and Botrytis cinerea (Liu et al, 1998). However, GOx has not been reported produced from Geotrichum genus.…”

Section: Introductionmentioning

confidence: 99%

“…For example, A. niger and P. amagasakiense show pH optima of 3.5 to 6.5 and 4.0 to 5.5, respectively (Nakamura and Fujiki, 1968). In contrast, the GOx obtained from P. sp CBS 120262 (Simpson et al, 2007), P. funiculosum 433 and P. canescens (Sukhacheva et al, 2004) show a slightly alkaline pH optima of 6 to 8.6. The lowest optimum temperature for GOx is reported to be 25-30°C from P. funiculosum 433 (Sukhacheva et al, 2004) with a highest optimum of 40 to 60°C from A. niger and P. amagasakiense ATCC 28686 (Kalisz et al, 1991).…”

mentioning

confidence: 97%

“…It has been reported that the fungal GOx is usually a dimmer enzyme with molecular weights ranging from approx. 130 to 175 kDa (Simpson et al, 2007;Kalisz et al, 1997), and consists of two identical polypeptide chain subunits covalently linked through disulfide bonds (Rando et al, 1997;Kalisz et al, 1997), though tetramer enzymes of GOx may also exist (Liu et al, 1998).…”

mentioning

confidence: 99%

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Purification and characterization of a novel glucose oxidase-like melanoidin decolorizing enzyme from Geotrichum sp. No. 56

Hwang¹,

YingShu²,

Sheu³

et al. 2011

Afr. J. Microbiol. Res.

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A novel melanoidin decolorizing enzyme (MDE) produced by Geotrichum sp. No. 56, which exhibits decolorization activity against synthetic melanoidin and molasses containing wastewater, was purified and characterized. The purification process was performed using ammonium sulfate fractionation, DEAE-Cellulose and Sephadex G-150 column chromatography. The melanoidin decolorization activity of the MDE was improved up to 7.3 U mg -1 , the equivalent to 8.3-fold increase from the initial protein preparation, with an overall yield of 9.1%. The results of gel filtration and SDS-PAGE revealed that the purified MDE was a dimmer with 127.5 kDa, and both subunits were alike with 63.5 kDa each. The optimum pH and temperature for the purified MDE were 6.5 and 45°C, respectively. The MDE activity was highly specific for -D-glucose, but completely inhibited by cysteine, iodoacetic acid, 2-mercaptoethanol, gluconic acid, HgCl 2 or AgNO 3 . The MDE also decolorized the spent broth of monosodium glutamate fermentation. The Geotrichum sp. No. 56 producing MDE, which shares various characteristics with glucose oxidase (GOx), could be useful for decolorizing fermented wastewater.

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Simultaneous utilization of glucose and gluconate in Penicillium chrysogenum during overflow metabolism

Schmitz

Peter

Meinert³

et al. 2013

Biotech & Bioengineering

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The filamentous fungus Penicillium chrysogenum is one of the most important production organism for β-lactam antibiotics, especially penicillin. A specific feature of P. chrysogenum is the formation of gluconate as the primary overflow metabolite under non-limiting growth on glucose. Gluconate can be formed extracellularly by the enzyme glucose oxidase (GOD) that shows high activities under glucose excess conditions. Currently, it is assumed that under these conditions glucose is the preferred carbon substrate for P. chrysogenum and gluconate consumption first starts after glucose becomes limiting. Here, we specifically address this hypothesis by combining batch cultivation experiments on defined glucose media, time-dependent GOD activity measurements, and (13)C-tracer studies. Our data prove that both substrates are metabolized simultaneously independent from the actual glucose concentration and therefore suggest that no distinct mechanism of carbon catabolite repression exists for gluconate in P. chrysogenum. Moreover, gluconate consumption does not interfere with penicillin V production by repression of the penicillin genes. Finally, by following a model-driven approach the specific uptake rates for glucose and gluconate were quantified and found to be significantly higher for gluconate. In summary, our results show that P. chrysogenum metabolizes gluconate directly and at high rates making it an interesting alternative carbon source for production purposes.

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Isolation, purification and characterization of a novel glucose oxidase from Penicillium sp. CBS 120262 optimally active at neutral pH

Cited by 37 publications

References 20 publications

Invertase, glucose oxidase and catalase for converting sucrose to fructose and gluconic acid through batch and membrane-continuous reactors

Invertase, glucose oxidase and catalase for converting sucrose to fructose and gluconic acid through batch and membrane-continuous reactors

Purification and characterization of a novel glucose oxidase-like melanoidin decolorizing enzyme from Geotrichum sp. No. 56

Simultaneous utilization of glucose and gluconate in Penicillium chrysogenum during overflow metabolism

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