Fermentative production of glucose oxidase from Aspergillus niger NCIM 545

Aim of this work was to establish the optimum conditions for the extraction and recovery by cationic reversed micelles of glucose oxidase (GOX) from Aspergillus niger A9, The influence of pH, temperature, solvent/co-solvents ratio on the extraction was investigated by experiment, using the residual enzyme activity to evaluate the results. The best condition for GOX extraction were ensured using iso-octane as solvent and butanol and n-hexanol co-solvent at 76/18/6 volume ratio, pH 4.80, 200mM cetyl-trimethyl ammonium bromide (CTAB) as cationic surfactant, The enzyme activity of GOX is measured by DNS method (3,5-dinitro salicylic acid method). In the extraction process, ultrasonic oscillation was adopted to mix organic solvent and water, ultrasonic oscillation temperature is 45 °C. Protein activity recovery of GOX can reach 88.2% in extraction.

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

Frontiers in Microbiology ◽

10.3389/fmicb.2018.02269 ◽

2018 ◽

Vol 9 ◽

Cited By ~ 2

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

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Effects of metal ions on simultaneous production of glucose oxidase and catalase by Aspergillus niger

Letters in Applied Microbiology ◽

10.1111/j.1472-765x.2001.00851.x ◽

2008 ◽

Vol 32 (1) ◽

pp. 16-19 ◽

Cited By ~ 1

Author(s):

J.-Z. Liu ◽

Y.-Y. Huang ◽

J. Liu ◽

L.-P. Weng ◽

L.-N. Ji

Keyword(s):

Aspergillus Niger ◽

Metal Ions ◽

Glucose Oxidase ◽

Simultaneous Production

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Corrections

Clinical Chemistry ◽

10.1093/clinchem/19.9.1084 ◽

1973 ◽

Vol 19 (9) ◽

pp. 1084-1084

Keyword(s):

Aspergillus Niger ◽

Horseradish Peroxidase ◽

Glucose Oxidase ◽

Gluconic Acid ◽

Type Ii ◽

Sigma Chemical

Abstract p 1424, Table 2, "units/liter" should read "milliunits/ liter." In reference to the article by Meites, S., and Saniel-Banrey, K., Clin. Chem. 19, 308 (1973), the authors wish to make the following clarification: The glucose oxidase used was purified from Aspergillus niger, and obtained from Sigma Chemical Co., St. Louis, Mo. 63178. It contained 1.5 EU/mg. One unit (EU) will oxidize 1 µmol of glucose to gluconic acid and H2O2 per minute at pH 5.1 at 35 °C. The peroxidase used was horseradish peroxidase and was obtained from Sigma Chemical Co. as Type II (RZ 1.0-1.5), approximately 100-150 Purpurogallin (20-s) Units/mg, or as Worthington "Peroxidase D," 626 U/mg (RZ > 1), Worthington Biochemical Corp., Freehold, N.J. 07728.

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