Partial Purification and Characterization of Sulfhydryl Oxidase from Aspergillus niger

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 exhibi...

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Bibliographic Details
Published in:Journal of food science 2002-08, Vol.67 (6), p.2016-2022
Main Authors: Vignaud, C, Kaid, N, Rakotozafy, L, Davidou, S, Nicolas, J
Format: Article
Language:English
Subjects:
Aspergillus niger
Biological and medical sciences
catalase
Chemistry
chromatography
cysteine
dithiothreitol
Food industries
Food science
Fundamental and applied biological sciences. Psychology
Fungi
homocysteine
isoelectric point
molecular weight
oxidation
properties
purification
sulfhydryl oxidase
Sulfide compounds
Use and upgrading of agricultural and food by-products. Biotechnology
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Summary: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 (V(mapp)/K(mapp)) increased from pH 4.5 to 6.5. At pH 5.6, the K(mapp)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(mapp)values represented 2, 34, 24, and 44% of the V(maPP)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.
ISSN:0022-1147
1750-3841
DOI:10.1111/j.1365-2621.2002.tb09494.x