Partial purification and characterization of sulfhydryl oxidase from Aspergillus niger

被引：8
|
作者：
Vignaud, C [1 ]
Kaid, N [1 ]
Rakotozafy, L [1 ]
Davidou, S [1 ]
Nicolas, J [1 ]
机构：
[1] Conservatoire Natl Arts & Metiers, Chaire Biochim Ind & Agro Alimentaire, F-75141 Paris 03, France
来源：
JOURNAL OF FOOD SCIENCE | 2002年 / 67卷 / 06期
关键词：
sulfhydryl oxidase; Aspergillus niger; purification; properties;
D O I：
10.1111/j.1365-2621.2002.tb09494.x
中图分类号：
TS2 [食品工业];
学科分类号：
0832 ;
摘要：
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 values represented 2, 34, 24, and 44% of the V-mapp value found for GSH, respectively. Cys-gly was not oxidize by SOX. In the presence of GSH, SOX is able to catalyze the oxidation of cysteine and cys-gly at a significant rate.
引用
收藏
页码：2016 / 2022
页数：7
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