Continuous Enzymatic Regeneration of Electron Acceptors Used by Flavoenzymes: Cellobiose Dehydrogenase-Catalyzed Production of Lactobionic Acid as an Example

Ludwig, Roland; Ozga, M.; Zámocký, Marcel; Peterbauer, Clemens K.; Kulbe, Klaus D.; Haltrich, Dietmar

doi:10.1080/10242420410001692787

Cited by 77 publications

(50 citation statements)

References 12 publications

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“…The broad range pI marker protein kit (pH 3-10; Serva) was used to determine the isoelectric point (pI). GDH bands were visualized by active staining with DCIP (Ludwig et al, 2004).…”

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confidence: 99%

Reduction of quinones and phenoxy radicals by extracellular glucose dehydrogenase from Glomerella cingulata suggests a role in plant pathogenicity

et al. 2011

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The plant-pathogenic fungus Glomerella cingulata (anamorph Colletotrichum gloeosporoides) secretes high levels of an FAD-dependent glucose dehydrogenase (GDH) when grown on tomato juice-supplemented media. To elucidate its molecular and catalytic properties, GDH was produced in submerged culture. The highest volumetric activity was obtained in shaking flasks after 6 days of cultivation (3400 U l "1 , 4.2 % of total extracellular protein). GDH is a monomeric protein with an isoelectric point of 5.6. The molecular masses of the glycoforms ranged from 95 to 135 kDa, but after deglycosylation, a single 68 kDa band was obtained. The absorption spectrum is typical for an FAD-containing enzyme with maxima at 370 and 458 nm and the cofactor is non-covalently bound. The preferred substrates are glucose and xylose. Suitable electron acceptors are quinones, phenoxy radicals, 2,6-dichloroindophenol, ferricyanide and ferrocenium hexafluorophosphate. In contrast, oxygen turnover is very low. The GDH-encoding gene was cloned and phylogenetic analysis of the translated protein reveals its affiliation to the GMC family of oxidoreductases. The proposed function of this quinone and phenoxy radical reducing enzyme is to neutralize the action of plant laccase, phenoloxidase or peroxidase activities, which are increased in infected plants to evade fungal attack.

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“…The broad range pI marker protein kit (pH 3-10; Serva) was used to determine the isoelectric point (pI). GDH bands were visualized by active staining with DCIP (Ludwig et al, 2004).…”

mentioning

confidence: 99%

Reduction of quinones and phenoxy radicals by extracellular glucose dehydrogenase from Glomerella cingulata suggests a role in plant pathogenicity

et al. 2011

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“…This might also be useful for protection of oxidases against air bubbles 4 which may promote enzyme inactivation 8,9 . The literature data suggests that gas bubbles cannot inactivate the enzymes immobilized on porous support 10,11 and that is why such support was chosen for this work [12][13][14] . In our previous work 14 operational stability of soluble porcine kidney DAAO was investigated during D-methionine oxidative deamination ( Fig.…”

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confidence: 99%

Stabilization of D-Amino Acid Oxidase via Covalent Immobilization and Mathematical Model of D-Methionine Oxidative Deamination Catalyzed by Immobilized Enzyme

Findrik

Tusić

Vasić-Rački

2016

Chem.Biochem.Eng.Q.

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Prigorje Brdovečko, Croatia (current position)Porcine kidney D-amino acid oxidase was stabilized by covalent immobilization on spherical particles of Eupergit C because of its low stability in soluble form. The focus of this work was to evaluate operational stability of the immobilized enzyme. To evaluate D-amino acid oxidase's operational stability during process conditions, repetitive batch reactor experiments of D-methionine oxidation reaction were carried out with continuous aeration for oxygen supply at air-flow rates of 5 and 10 dm 3 h -1 . Kinetic analysis of the immobilized enzyme was done as well. The mathematical model of D-methionine oxidative deamination catalyzed by the immobilized D-amino acid oxidase was developed and it described the data well. It enabled the estimation of operational stability decay rate constant. It was possible to achieve 100 % substrate conversion in all batch experiments.

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“…Therefore, fungal enzymes, carbohydrate: acceptor oxidoreductase, [12][13][14] glucooligosaccharide oxidase, 16,17) and cellobiose dehydrogenase 15) have been studied in connection with the production of LacA. Other bacteria, Pseudomonas aeruginosa 6) and Burkholderia cepacia, [7][8][9] also have been studied for LacA production.…”

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confidence: 99%

“…[1][2][3] It has been reported to increase intestinal calcium absorption, 4,5) suggesting that it might be possible to use LacA for health benefit in foods. There have been a number of studies focusing on lactose-oxidizing bacteria, [6][7][8][9][10][11] fungi, [12][13][14][15][16][17] and red algae. 18) Most of these organisms, however, are difficult to use in the production of LacA for foods.…”

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confidence: 99%

Optimization of Lactobionic Acid Production byAcetobacter orientalisIsolated from Caucasian Fermented Milk, “Caspian Sea Yogurt”

Kiryu

Yamauchi

Masuyama

et al. 2012

Bioscience, Biotechnology, and Biochemistry

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Continuous Enzymatic Regeneration of Electron Acceptors Used by Flavoenzymes: Cellobiose Dehydrogenase-Catalyzed Production of Lactobionic Acid as an Example

Cited by 77 publications

References 12 publications

Reduction of quinones and phenoxy radicals by extracellular glucose dehydrogenase from Glomerella cingulata suggests a role in plant pathogenicity

Reduction of quinones and phenoxy radicals by extracellular glucose dehydrogenase from Glomerella cingulata suggests a role in plant pathogenicity

Stabilization of D-Amino Acid Oxidase via Covalent Immobilization and Mathematical Model of D-Methionine Oxidative Deamination Catalyzed by Immobilized Enzyme

Optimization of Lactobionic Acid Production byAcetobacter orientalisIsolated from Caucasian Fermented Milk, “Caspian Sea Yogurt”

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