Optimization of an Aspergillus niger glucose oxidase production process

Rothberg, Anette; Weegar, Jan; Schalien, Randolf von; Fagervik, Kaj; Rydström, Mikael; Lind, Kirsten E.

doi:10.1007/pl00009075

Cited by 9 publications

(2 citation statements)

References 15 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Early studies on A. niger GOX production and purification treated the enzyme as intracellular [13][14][15], a fact supported by the claim of its localization in peroxisomes [16]. While there also appeared reports dealing with the optimization of GOX production from A. niger measuring only the extracellular levels of the enzyme [17,18], the prevalent viewpoint on the matter is that the enzyme is mostly cell associated and it appears in the extracellular medium as a result of an active secretion process, a situation described for both wild-type [19][20][21][22] and recombinant A. niger strains [23,24]. The above fact is also supported by immunocytochemical studies that revealed that the bulk of the enzyme is localized in the cell wall [25].…”

Section: Introductionmentioning

confidence: 93%

Cell Bound and Extracellular Glucose Oxidases from Aspergillus niger BTL: Evidence for a Secondary Glycosylation Mechanism

Hatzinikolaou¹,

Mamma

Christakopoulos

et al. 2007

Appl Biochem Biotechnol

View full text Add to dashboard Cite

Two glucose oxidase (GOX) isoforms where purified to electrophoretic homogeneity from the mycelium extract (GOXI) and the extracellular medium (GOXII) of Aspergillus niger BTL cultures. Both enzymes were found to be homodimers with nonreduced molecular masses of 148 and 159 kDa and pI values of 3.7 and 3.6 for GOXI and GOXII, respectively. The substrate specificity and the kinetic characteristics of the two GOX forms, as expressed through their apparent K m values on glucose, as well as pH and T activity optima, were almost identical. The only structural difference between the two enzymes was in their degrees of glycosylation, which were determined equal to 14.1 and 20.8% (w/w) of their molecular masses for GOXI and GOXII, respectively. The above difference in the carbohydrate content between the two enzymes seems to influence their pH and thermal stabilities. GOXII proved to be more stable than GOXI at pH values 2.5, 3.0, 8.0, and 9.0. Half-lives of GOXI at pH 3.0 and 8.0 were 8.9 and 17.5 h, respectively, whereas the corresponding values for GOXII were 13.5 and 28.1 h. As far as the thermal stability is concerned, GOXII was also more thermostable than GOXI as judged by the deactivation constants determined at various temperatures. More specifically, the half-lives of GOXI and GOXII, at 45 degrees C, were 12 and 49 h, respectively. These results suggest A. niger BTL probably possesses a secondary glycosylation mechanism that increases the stability of the excreted GOX.

show abstract

Section: Introductionmentioning

confidence: 93%

Cell Bound and Extracellular Glucose Oxidases from Aspergillus niger BTL: Evidence for a Secondary Glycosylation Mechanism

Hatzinikolaou¹,

Mamma

Christakopoulos

et al. 2007

Appl Biochem Biotechnol

View full text Add to dashboard Cite

show abstract

“…The effects of different mutants of A. niger strains on GO production were reported in the literature. [31,32] This indicates that different strains of the same microorganism may exhibit fundamental metabolic differences even if the same metabolite is produced.…”

Section: Selection Of a Niger Isolates For Go Production On Rhpmmentioning

confidence: 98%

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

Joint effect of nitrogen and phosphorous on glucose oxidase production by Aspergillus niger: Discussion of an experimental design with a risk of co-linearity

Mirón

Vázquez

González

et al. 2008

Biochemical Engineering Journal

View full text Add to dashboard Cite

Optimization of an Aspergillus niger glucose oxidase production process

Cited by 9 publications

References 15 publications

Cell Bound and Extracellular Glucose Oxidases from Aspergillus niger BTL: Evidence for a Secondary Glycosylation Mechanism

Cell Bound and Extracellular Glucose Oxidases from Aspergillus niger BTL: Evidence for a Secondary Glycosylation Mechanism

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

Joint effect of nitrogen and phosphorous on glucose oxidase production by Aspergillus niger: Discussion of an experimental design with a risk of co-linearity

Contact Info

Product

Resources

About