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- Title
Induction, purification and molecular characterization of sulfhydryl oxidase from an Egyptian isolates of Aspergillus niger.
- Authors
Moubasher, H.; Fahmi, A.; Abdur-Rahman, M.
- Abstract
The conditions for the sulfhydryl oxidase (SOX) production and activity from an Egyptian isolate of Aspergillus niger were optimized. Purification and determination of the kinetic properties ( K and V) of the purified enzyme have been done. The possibility for the SOX induction using L-Cys (as a natural substrate) was studied to determine whether SOX could be produced as an inducible enzyme in addition to being a constitutive one (i.e. whether induction leads to increase SOX production and activity or not). The optimum temperature and pH for its activity were found to be 60°C and 5.5, respectively. The activity of the induced intracellular SOX, was measured according to Ellman's method using the standard GSH oxidation where it reached 94% while that of non-induced one reached only 27.6%. This wide difference in activity between the induced and non-induced SOX indicates the successful L-Cys-induction of the SOX production (i.e. SOX from A. niger AUMC 4947 is an inducible enzyme). Molecular characterization of the pure SOX revealed that it is constituted of two 50-55 KDa subunits. K and V were found to be 6.0 mM and 100 μM/min/mg respectively.
- Subjects
SULFHYDRYL oxidases; ASPERGILLUS niger; ENZYMES; TEMPERATURE; HYDROGEN-ion concentration; OXIDATION; GLUTATHIONE; ASPERGILLUS
- Publication
Applied Biochemistry & Microbiology, 2012, Vol 48, Issue 3, p290
- ISSN
0003-6838
- Publication type
Article
- DOI
10.1134/S000368381203009X