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Optimization and Production of Glucose Oxidase from a newly isolated strain of Aspergillus fumigatus

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DOI: 10.23977/enzyme.2022.010103 | Downloads: 65 | Views: 1632

Author(s)

Onosakponome I 1, Okwuenu P 1, Oparaji E 1, Ezugwu A.L 1, Eze S.O.O 1, Chilaka, F.C 1

Affiliation(s)

1 Department of Biochemistry, University of Nigeria, Nsukka, Enugu State, Nigeria

Corresponding Author

Onosakponome I

ABSTRACT

Glucose oxidase (GOx) has several novel applications in chemical, pharmaceutical, textile, and other biotechnological industries. This study was aimed at optimizing the production of glucose oxidase from Aspergillus fumigatus AFS4. Aspergillus fumigatus was isolated from garden soil, obtained from staff quarters University of Nigeria, Nsukka and was screened for glucose oxidase production capability.  Biochemical tests and 18S-rDNA sequencing were used to confirm the isolate as Aspergillus fumigatus. The isolate strain was tagged as Aspergillus fumigatus AFS4. GOx was produced from Aspergillus fumigatus AFS4 under submerged fermentation system with an enzyme activity of 1591Uµmol/min and protein concentration of 3.89mg/ml. Different conditions for GOx production which include carbon sources, nitrogen sources, CaCO3, pH and fermentation time were optimized. Glucose (80g/L) was found to be the best carbon source for GOx production with GOx activity of 1542µmol/min. Peptone (3g/L) was found suitable for GOx production with GOx activity of 1231µmol/min compared to other nitrogen sources tested. CaCO3 enhanced GOx production when 30g/L of it was used to supplement the production medium. The optimum pH for GOx production was 6.5.  The highest GOx production was obtained on the 7th day with GOx activity of 1517µmol/min. The results proved that Aspergillus fumigatus AFS4 has strong potential to produce glucose oxidase for various industrial applications. 

KEYWORDS

Isolation, Aspergillus fumigatus AFS4, 18S-rDNA sequence, Optimization, Glucose oxidase

CITE THIS PAPER

Onosakponome I., Okwuenu P., Oparaji E., Ezugwu A.L., Eze S.O.O. and Chilaka, F.C., Optimization and Production of Glucose Oxidase from a newly isolated strain of Aspergillus fumigatus. Journal of Enzyme Engineering (2022) Vol. 1: 39-48. DOI: http://dx.doi.org/10.23977/enzyme.2022.010103.

REFERENCES

[1] Bankar, S., Bule, M., Singhal, R. Ananthanarayan, L. (2008). Optimization of Aspergillus Niger fermentation for the production of glucose oxidase. Food Bioprocess Technology, 19: 47-56.
[2] Bankar, S., Bule, M., Singhal, R. and Ananthanarayan, L. (2009). Glucose oxidase — An overview, Biotechnology Advances, 27: 489–501.
[3] Bao, J., Koumatsu, K., Arimatsu, Y., Furumoto, K., Yoshimoto, M., Fukunaga, K., and Nakao, K., (2003). A kinetic study on crystallization of calcium gluconate in external loop airlift column and stirred tank for an immobilized glucose oxidase reaction with crystallization. Biochemical Engineering Journal, 15:177-184
[4] Bergmeyer, H., Gawehn, K. and Grassl, M. (1974).  Methods of Enzymatic Analysis Bergmeyer, HU, Second Edition, vol. 1. New York: Academic Press Inc.; p. 457–8.
[5] Clark, D.S., Bordner, P., Galdrich, E.H., kabler, P.W. and Huff, C.B. (1958). Applied Microbiology International Book Company. New York, 27-53pp.
[6] Eun-Ha, P., Young-Mi, S., Young-Yi, L., Tae-Ho, K., Dae-Hyuk, K. and Moon-Sik Y. (2000). Expression of glucose oxidase by using recombinant yeast. Journal of Biotechnology 81: 35–44.
[7] Fiedurek, J. and Gromada, A. (2000). Production of catalase and glucose oxidase by Aspergillus Niger using unconventional oxygenation of culture. Journal of Applied Microbiology, 89(1): 85-89.
[8] Liu, J., Huang, Y., Liu, J., Weng, L. and Ji, L. (2001a). Effects of metal ions on simultaneous production of glucose oxidase and catalase by Aspergillus Niger. Letter of Applied Microbiology, 32:16–19.
[9] Lowry, O. H., Rosebrough, N.J., Farr, A. L. and Randell, R. J. (1951). Protein measurement with the folin phenol reagent. Journal of Biological Chemistry, 193: 265- 275
[10] Martin, N., de Souza, S.R., da Silva, R. and Gomes, E. (2004). Pectinase production of fungal strains in solid state fermentation using agfro-industrial bioproduct. Brazillian archives of Biology and Technology, 47(5): 813-819.
[11] Mirón, J., González, M. P., Pastrana, L., and Murado, M. A. (2002). Diauxic production of glucose oxidase by Aspergillus Niger in submerged culture a dynamic model. Enzyme and Microbial Technology, 31:615–620
[12] Mukhtar, H. Ikram, H., Ali, N., and Waseem, A. (2014). .Isolation and Identification of Glucose Oxidase Hyper Producing Strain of Aspergillus Niger. British Microbiology Research Journal 4(2): 195-205.
[13] Müller, D. (1928). Oxidation von Glukose mit Extrakten aus Aspegillus Niger. Biochem. Z. 199:136–170.
[14] Sathiya, M. (2009). Optimization, Characterization and Applications of Glucose Oxidase produced from Aspergillus awamori MTCC 9645 for food processing and preservation. A PhD thesis submitted to Educational and Research Institute University, Chennai.
[15] Silva, R.D.N., Quintino, F. P., Monteiro, V.N. and Asquieri, E.R. (2010). Production of glucose and fructose syrups from cassava (Manihot esulenta Crantz) starch using enzymes produced by microorganisms isolated from Brazilian Cerrado soil. Food Science and Technology, 30(1): 213-217.
[16] Simpson C, Jordaan J, Gardiner NS and Whiteley C (2006). Isolation, purification and characterization of a novel glucose oxidase from Penicillium sp. CBS 120262 optimally active at neutral pH, doi:10.1016/j.pep.2006.09.013.    
[17]Singh, J. and Verma. N. (2013). Glucose oxidase from Aspergillus Niger: Production, characterization and immobilization for glucose oxidation. Advances in Applied Science Research, 4(3):250-257.
[18] Todde, G., Hovmöller, S., Laaksonen, A., and Mocc, F. (2014). Glucose oxidase from Penicillium amagasakiense: characterization of the transition state of its denaturation from molecular dynamics simulations. Proteins 82:2353–2363. 
[19] Xu, G., Xu, Y., Li, A., Chen, T., and Liu, J. (2017). Enzymatic bioactivity investigation of glucose oxidase modified with hydrophilic or hydrophobic polymers via in situ RAFT polymerization. Journal of Polymer Science A: Polymer Chemistry, 55:1289–1293.

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