scholarly journals Forward Genetics by Genome Sequencing Uncovers the Central Role of the Aspergillus niger goxB Locus in Hydrogen Peroxide Induced Glucose Oxidase Expression

2018 ◽  
Vol 9 ◽  
Author(s):  
Thanaporn Laothanachareon ◽  
Juan Antonio Tamayo-Ramos ◽  
Bart Nijsse ◽  
Peter J. Schaap
Keyword(s):  
Hydrogen Peroxide ◽  
Aspergillus Niger ◽  
Glucose Oxidase ◽  
Genome Sequencing ◽  
Forward Genetics

scholarly journals Expression of Aspergillus niger glucose oxidase in Pichia pastoris and its antimicrobial activity against Agrobacterium and Escherichia coli

PeerJ ◽  
2020 ◽  
Vol 8 ◽  
pp. e9010
Author(s):  
Yonggang Wang ◽  
Jiangqin Wang ◽  
Feifan Leng ◽  
Jianzhong Ma ◽  
Alnoor Bagadi
Keyword(s):  
Escherichia Coli ◽  
Hydrogen Peroxide ◽  
Aspergillus Niger ◽  
Pichia Pastoris ◽  
Glucose Oxidase ◽  
Fermentation Medium ◽  
Logarithmic Phase ◽  
Transgenic Strain ◽  
E Coli ◽  
Cell Lysate

The gene encoding glucose oxidase from Aspergillus niger ZM-8 was cloned and transferred to Pichia pastoris GS115, a transgenic strain P. pastoris GS115-His-GOD constructed. The growth curve of P. pastoris GS115-His-GOD was consistent with that of Pichia pastoris GS115-pPIC9K under non-induced culture conditions. Under methanol induction conditions, the growth of the GOD-transgenic strain was significantly lowered than P. pastoris GS115-pPIC9K with the induced-culture time increase, and the optical densities of GOD-transgenic strain reached one-third of that of the P. pastoris GS115-pPIC9K at 51 h. The activity of glucose oxidase in the cell-free supernatant, the supernatant of cell lysate, and the precipitation of cell lysate was 14.3 U/mL, 18.2 U/mL and 0.48 U/mL, respectively. The specific activity of glucose oxidase was 8.3 U/mg, 6.52 U/mg and 0.73 U/mg, respectively. The concentration of hydrogen peroxide formed by glucose oxidase from supernatant of the fermentation medium, the supernatant of the cell lysate, and the precipitation of cell lysate catalyzing 0.2 M glucose was 14.3 μg/mL, 18.2 μg/mL, 0.48 μg/mL, respectively. The combination of different concentrations of glucose oxidase and glucose could significantly inhibit the growth of Agrobacterium and Escherichia coli in logarithmic phase. The filter article containing supernatant of the fermentation medium, supernatant of the cell lysate, and precipitation of cell lysate had no inhibitory effect on Agrobacterium and E. coli. The minimum inhibitory concentration of hydrogen peroxide on the plate culture of Agrobacterium and E. coli was 5.6 × 103 μg/mL and 6.0 × 103 μg/mL, respectively.

METABOLISM OF MAMMALIAN ERYTHROCYTES: V. ROLE OF CATALASE IN THE OXIDATION OF RIBOSE-5-PHOSPHATE BY THE ERYTHROCYTE

1954 ◽  
Vol 32 (6) ◽  
pp. 644-654 ◽  
Author(s):  
Marc Francoeur ◽  
Orville F. Denstedt
Keyword(s):  
Hydrogen Peroxide ◽  
Methylene Blue ◽  
Glucose Oxidase ◽  
Anaerobic Conditions ◽  
Beef Liver ◽  
Aerobic Conditions

Ribose-5-phosphate has been found to be rapidly oxidized by the stroma-free hemolyzate of human, rat, and rabbit erythrocytes in the presence of ferricyanide under anaerobic conditions, or in the presence of methylene blue under aerobic conditions. Compounds resembling R-5-P, such as ribose, arabinose, xylose, glucose, glucose-6-phosphate, fructose-6-phosphate, and hexose diphosphate are not oxidized under these conditions. The oxidation does not involve DPN or TPN and it is completely inhibited by cyanide. The Ks is about 2 × 10−2 M. Under anaerobic conditions, in the presence of ferricyanide, the enzyme responsible for the oxidation is catalase. Purified catalase from beef liver or from rabbit erythrocytes yields the same results as the SFH from human, rat, or rabbit erythrocytes with respect to specificity, cyanide sensitivity, and the Ks value. Under aerobic conditions, catalase is responsible also for the oxidation of R-5-P, but the mechanism involves the peroxidase action of catalase. Catalase catalyzes the oxidation of R-5-P by hydrogen peroxide in the presence of a system which slowly generates hydrogen peroxide, such as the glucose–glucose oxidase or the hemoglobin – methylene blue systems.

Effect of deglycosylation of N-linked sugar chains on glucose oxidase from Aspergillus niger

1989 ◽  
Vol 67 (8) ◽  
pp. 460-464 ◽  
Author(s):  
Kaoru Takegawa ◽  
Kentaro Fujiwara ◽  
Shojiro Iwahara ◽  
Kenji Yamamoto ◽  
Tatsurokuro Tochikura
Keyword(s):  
Aspergillus Niger ◽  
Glucose Oxidase ◽  
Ammonium Sulfate ◽  
Trichloroacetic Acid ◽  
Enzyme Stability ◽  
High Solubility ◽  
Catalytic Activities ◽  
Carbohydrate Depletion ◽  
Sugar Chains

Endo-β-N-acetylglucosaminidase from Flavobacterium sp. released about 30% of the N-linked sugar chains from the glucose oxidase of Aspergillus niger. To elucidate the role of the carbohydrate moiety, the enzymatic properties of native and carbohydrate-depleted glucose oxidases were compared. It was found that their catalytic activities and thermal and pH stabilities were identical. However, the carbohydrate-depleted glucose oxidase was more rapidly precipitated by the addition of trichloroacetic acid and ammonium sulfate than the native enzyme. These results show that the N-linked sugar chains of the glucose oxidase contributed to the high solubility of the enzyme in water.Key words: glucose oxidase, Aspergillus niger, carbohydrate depletion, endo-β-N-acetylglucosaminidase, enzyme stability.

A novel nanoplatform encapsulating glucose oxidase for spectrophotometric biosensing of hydrogen peroxide and glucose

2020 ◽  
Vol 12 (3) ◽  
pp. 345-357
Author(s):  
Hamzeh Pezhhan ◽  
Morteza Akhond ◽  
Mojtaba Shamsipur
Keyword(s):  
Hydrogen Peroxide ◽  
Glucose Oxidase ◽  
Protein Interactions ◽  
Magnetic Nanoparticle ◽  
Marine Mussels

Inspired by the role of the chelation of Fe3+–catechol in inter-protein interactions and the production of adhesives by marine mussels, we used DA as an anchor to connect GOx to Fe3O4 magnetic nanoparticle cores via the formation of Fe(OH)3 shells.

METABOLISM OF MAMMALIAN ERYTHROCYTES: V. ROLE OF CATALASE IN THE OXIDATION OF RIBOSE-5-PHOSPHATE BY THE ERYTHROCYTE

1954 ◽  
Vol 32 (1) ◽  
pp. 644-654 ◽  
Author(s):  
Marc Francoeur ◽  
Orville F. Denstedt
Keyword(s):  
Hydrogen Peroxide ◽  
Methylene Blue ◽  
Glucose Oxidase ◽  
Anaerobic Conditions ◽  
Beef Liver ◽  
Aerobic Conditions

Ribose-5-phosphate has been found to be rapidly oxidized by the stroma-free hemolyzate of human, rat, and rabbit erythrocytes in the presence of ferricyanide under anaerobic conditions, or in the presence of methylene blue under aerobic conditions. Compounds resembling R-5-P, such as ribose, arabinose, xylose, glucose, glucose-6-phosphate, fructose-6-phosphate, and hexose diphosphate are not oxidized under these conditions. The oxidation does not involve DPN or TPN and it is completely inhibited by cyanide. The Ks is about 2 × 10−2 M. Under anaerobic conditions, in the presence of ferricyanide, the enzyme responsible for the oxidation is catalase. Purified catalase from beef liver or from rabbit erythrocytes yields the same results as the SFH from human, rat, or rabbit erythrocytes with respect to specificity, cyanide sensitivity, and the Ks value. Under aerobic conditions, catalase is responsible also for the oxidation of R-5-P, but the mechanism involves the peroxidase action of catalase. Catalase catalyzes the oxidation of R-5-P by hydrogen peroxide in the presence of a system which slowly generates hydrogen peroxide, such as the glucose–glucose oxidase or the hemoglobin – methylene blue systems.

Susceptibility to hydrogen peroxide ofPlasmodium falciparuminfecting glucose-6-phosphate dehydrogenase-deficient erythrocytes

Parasitology ◽  
1989 ◽  
Vol 99 (2) ◽  
pp. 171-174 ◽  
Author(s):  
S. Kamchonwongpaisan ◽  
A. Bunyaratvej ◽  
W. Wanachiwanawin ◽  
Y. Yuthavong
Keyword(s):  
Hydrogen Peroxide ◽  
Plasmodium Falciparum ◽  
Glucose Oxidase ◽  
Host Cells ◽  
Parasite Invasion ◽  
Killing Effect ◽  
Oxidase System ◽  
Relative Susceptibility ◽  
Glucose 6 Phosphate Dehydrogenase

SummaryThe susceptibility to oxidant-mediated killing ofPlasmodium falciparuminfecting normal and glucose-6-phosphate dehydrogenase (G6PD)-deficient erythrocytes was assessed by exposure to hydrogen peroxide generated by the glucose–glucose oxidase system. The parasites infecting G6PD-deficient erythrocytes had markedly greater susceptibility to hydrogen peroxide under a variety of conditions than those infecting normal erythrocytes. In both cases, the killing effect was mediated mainly through the host cells since treatment of the erythrocytes with hydrogen peroxide did not change their relative susceptibility. The parasites were most susceptible during maturation, especially in G6PD-deficient erythrocytes, although a reduction in parasite invasion was also observed. The role of oxidant-mediated killing in the protection of G6PD-deficient hosts fromP. falciparuminfection is discussed.

The role of copper ions in hydrogen peroxide bleaching: Their origin, removal, and effect on pulp quality

TAPPI Journal ◽  
2012 ◽  
Vol 11 (7) ◽  
pp. 37-46 ◽  
Author(s):  
PEDRO E.G. LOUREIRO ◽  
SANDRINE DUARTE ◽  
DMITRY V. EVTUGUIN ◽  
M. GRAÇA V.S. CARVALHO
Keyword(s):  
Hydrogen Peroxide ◽  
Copper Ions ◽  
Peroxide Bleaching ◽  
Metals Removal ◽  
Peroxide Decomposition ◽  
Equipment Corrosion ◽  
And Performance ◽  
And Control ◽  
Main Effects

This study puts particular emphasis on the role of copper ions in the performance of hydrogen peroxide bleaching (P-stage). Owing to their variable levels across the bleaching line due to washing filtrates, bleaching reagents, and equipment corrosion, these ions can play a major role in hydrogen peroxide decomposition and be detrimental to polysaccharide integrity. In this study, a Cu-contaminated D0(EOP)D1 prebleached pulp was subjected to an acidic washing (A-stage) or chelation (Q-stage) before the alkaline P-stage. The objective was to understand the isolated and combined role of copper ions in peroxide bleaching performance. By applying an experimental design, it was possible to identify the main effects of the pretreatment variables on the extent of metals removal and performance of the P-stage. The acid treatment was unsuccessful in terms of complete copper removal, magnesium preservation, and control of hydrogen peroxide consumption in the following P-stage. Increasing reaction temperature and time of the acidic A-stage improved the brightness stability of the D0(EOP)D1AP bleached pulp. The optimum conditions for chelation pretreatment to maximize the brightness gains obtained in the subsequent P-stage with the lowest peroxide consumption were 0.4% diethylenetriaminepentaacetic acid (DTPA), 80ºC, and 4.5 pH.

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