Thermal Characterization of Purified Glucose Oxidase from A Newly Isolated Aspergillus Niger UAF-1

Zia, Muhammad Anjum; Rahman, Khalilur; Saeed, Muhammad; Andaleeb, Fozia; Rajoka, Muhammad Ibrahim; Sheikh, Munir A.; Khan, Iftikhar Ahmad; Khan, Azeem Iqbal

doi:10.3164/jcbn.2007018

Cited by 20 publications

(12 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The GOX activity-versus-pH profile, shown by the enzyme produced in K. marxianus , was closer to the standard enzyme in the range between the values of 3 and 7, when compared to the GOX produced by K. lactis . An optimum pH value of 5.5 was obtained by Zia et al [ 32 ]. In alkaline pH values, the standard GOX is slightly more active than the ones expressed in either K. marxianus or K. lactis .…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Heterologous expression of glucose oxidase in the yeast Kluyveromyces marxianus

et al. 2010

View full text Add to dashboard Cite

BackgroundIn spite of its advantageous physiological properties for bioprocess applications, the use of the yeast Kluyveromyces marxianus as a host for heterologous protein production has been very limited, in constrast to its close relative Kluyveromyces lactis. In the present work, the model protein glucose oxidase (GOX) from Aspergillus niger was cloned into K. marxianus CBS 6556 and into K. lactis CBS 2359 using three different expression systems. We aimed at verifying how each expression system would affect protein expression, secretion/localization, post-translational modification, and biochemical properties.ResultsThe highest GOX expression levels (1552 units of secreted protein per gram dry cell weight) were achieved using an episomal system, in which the INU1 promoter and terminator were used to drive heterologous gene expression, together with the INU1 prepro sequence, which was employed to drive secretion of the enzyme. In all cases, GOX was mainly secreted, remaining either in the periplasmic space or in the culture supernatant. Whereas the use of genetic elements from Saccharomyces cerevisiae to drive heterologous protein expression led to higher expression levels in K. lactis than in K. marxianus, the use of INU1 genetic elements clearly led to the opposite result. The biochemical characterization of GOX confirmed the correct expression of the protein and showed that K. marxianus has a tendency to hyperglycosylate the protein, in a similar way as already observed for other yeasts, although this tendency seems to be smaller than the one of e.g. K. lactis and S. cerevisiae. Hyperglycosylation of GOX does not seem to affect its affinity for the substrate, nor its activity.ConclusionsTaken together, our results indicate that K. marxianus is indeed a good host for the expression of heterologous proteins, not only for its physiological properties, but also because it correctly secretes and folds these proteins.

show abstract

Section: Resultsmentioning

confidence: 99%

“…Wong et al [ 29 ] reviewed several authors who published values ranging from 33 mM (at 25°C) to 248 mM (at 30°C). Zia et al published a K M of 2.56 mM (at 40°C) for a GOX produced by A. niger UAF-1 [ 32 ]. The same authors obtained a K M of 28 mM for the enzyme produced by A. niger BCG-5, a gamma radiation-mutant strain [ 34 ].…”

Section: Resultsmentioning

confidence: 99%

Heterologous expression of glucose oxidase in the yeast Kluyveromyces marxianus

et al. 2010

View full text Add to dashboard Cite

show abstract

“…GOD was widely used as a potent antibacterial and antifungal agent in the food industry [12][13][14]. It is capable of inhibiting the growth of microorganisms through naturally produced hydrogen peroxide and gluconic acid [15]. Thus, the H 2 O 2 cytotoxicity and the lowering of pH by the production of Dgluconic acid may influence the growth of some microorganisms [16].…”

Section: Introductionmentioning

confidence: 99%

Biocontrol of tomato plant diseases caused by Fusarium solani using a new isolated Aspergillus tubingensis CTM 507 glucose oxidase

Kriaa

Hammami

Sahnoun

et al. 2015

Comptes Rendus. Biologies

View full text Add to dashboard Cite

The present study focuses on the potential of glucose oxidase (GOD) as a promising biocontrol agent for fungal plant pathogens. In fact, a new GOD producing fungus was isolated and identified as an Aspergillus tubingensis. GOD (125 AU) has been found to inhibit Fusarium solani growth and spore production. Indeed, GOD caused the reduction of spores, the formation of chlamydospores, the induction of mycelial cords and the vacuolization of mycelium. In vivo assays, GOD acted as a curative treatment capable of protecting the tomato plants against F. solani diseases. In fact, the incidence was null in the curative treatment with GOD and it is around 45% for the preventive treatment. The optimization of media composition and culture conditions led to a 2.6-fold enhancement in enzyme activity, reaching 81.48U/mL. This study has demonstrated that GOD is a potent antifungal agent that could be used as a new biofungicide to protect plants from diseases.

show abstract

“…It is also used in preventing rancidity in mayonnaise, as a source of hydrogen peroxide in food preservation, and in gluconic acid production; in quantitative analysis of glucose; and in medical diagnostics, medicine, and scientific research. [4][5][6][7][8][9] It is recommended that this list of functions of GO includes mention of its importance in sustainable energy production and bioprocessing, such as fuel cell applications, as in Wong et al (2008) [3] and Gomez et al (2010). [10] The mycelial fungi Aspergillus niger, Penicillium amagasakiense, and P. notatum serve as industrial producers of GO.…”

Section: Introductionmentioning

confidence: 99%

“…[10] The mycelial fungi Aspergillus niger, Penicillium amagasakiense, and P. notatum serve as industrial producers of GO. [9] Although several organisms have been reported to produce GO, [11,12] Aspergillus niger is the main organism used for industrial production. [13] In addition, the GO from Aspergillus niger is the basis of many industrial applications.…”

Section: Introductionmentioning

confidence: 99%

UTILIZATION OF RAM HORN PEPTONE IN THE PRODUCTION OF GLUCOSE OXIDASE BY A LOCAL ISOLATEAspergillus nigerOC-3

Canli

Kurbanoğlu

2010

Preparative Biochemistry and Biotechnology

View full text Add to dashboard Cite

Glucose oxidase (GO) is an enzyme that is used in many fields. In this study, ram horn peptone (RHP) was utilized as the nitrogen source and compared with other nitrogen sources in the production of GO by Aspergillus niger. To obtain higher GO activity, 14 A. niger strains were isolated from soil samples around Erzurum, Turkey. Among these strains, the isolate that was named A. niger OC-3 achieved the highest GO production. The production of GO was carried out in 100 mL scaled batch culture. The fermentation conditions such as initial pH, temperature, agitation speed, and time were investigated in order to improve GO production. The results showed that the cultivation conditions would significantly affect the formation of GO, and the utilization of the RHP achieved the highest enzyme production (48.6 U/mL) if compared to other nitrogen sources. On the other hand, the maximum biomass was obtained by using the fish peptone (7.2 g/L), while RHP yielded 6.4 g/L. These results suggest that RHP from waste ram horns could effectively be used in the production of GO by A. niger OC-3.

show abstract

Thermal Characterization of Purified Glucose Oxidase from A Newly Isolated Aspergillus Niger UAF-1

Cited by 20 publications

References 34 publications

Heterologous expression of glucose oxidase in the yeast Kluyveromyces marxianus

Heterologous expression of glucose oxidase in the yeast Kluyveromyces marxianus

Biocontrol of tomato plant diseases caused by Fusarium solani using a new isolated Aspergillus tubingensis CTM 507 glucose oxidase

UTILIZATION OF RAM HORN PEPTONE IN THE PRODUCTION OF GLUCOSE OXIDASE BY A LOCAL ISOLATEAspergillus nigerOC-3

Contact Info

Product

Resources

About