Isolation and Purification of Methyl Mercaptan Oxidase from Thiobacillus thiooxidans for Detection of Mercaptans
2000
Kim Sang-Joon | yang Ji-Won KAIST, Taejon (Korea Republic)
Methyl mercaptan oxidase was isolated and purified from Thiobacillus thiooxidans KCTC2505 for the detection of mercaptans. The procedure of purification involved DEAE-Sephacel and Superose 12 column chromatographies with recovery yields of 40 and 6.3%, and specific activity of 19.7 and 80.1 units/mg-protein, respectively. The molecular weight of purified methyl mercaptan oxidase was determined to be 68.1 kDa by SDS-PAGE. The extract from DEAE-Sephacel column chromatography had a high activity in oxidizing methyl mercaptan to produce formaldehyde which can be easily detected by purpald-coloring method. Optimum temperature for activity was observed at 43 degrees. This enzyme was activated by NH4CI and (NH4)2HO4, and inhibited by KCI and NaCI.
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