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- Title
Partial Purification and Characterization of Sulfhydryl Oxidase from Aspergillus niger.
- Authors
Vignaud, C.; Kaid, N.; Rakotozafy, L.; Davidou, S.; Nicolas, J.
- Abstract
Sulfhydryl oxidase (SOX) was purified after extraction and the contaminating catalase activity was completely eliminated in the last chromatography step. A yield of 25% was obtained with a purification factor higher than 300. The isoelectric point was 3.7 and the molecular weight 110 kDa. SOX exhibited an optimal activity at pH 5.6 and its efficiency (Vmapp/Kmapp) increased from pH 4.5 to 6.5. At pH 5.6, the Kmapp values were 0.5, 2.5, 10.5, 110, and 450 mM for GSH, cysteine, g-glu-cys, dithiothreitol, and homocysteine, respectively, and the V values represented 2, 34, 24, and 44% of the Vmapp value found for GSH, respectively. Cys-gly was not oxidized by SOX. In the presence of GSH, SOX is able to catalyze the oxidation of cysteine and cys-gly at a significant rate.
- Subjects
ASPERGILLUS niger; SULFHYDRYL oxidases; CATALASE; HYDROGEN-ion concentration; ASPERGILLUS
- Publication
Journal of Food Science (Wiley-Blackwell), 2002, Vol 67, Issue 6, p2016
- ISSN
0022-1147
- Publication type
Article
- DOI
10.1111/j.1365-2621.2002.tb09494.x