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铁道科学与工程学报

JOURNAL OF RAILWAY SCIENCE AND ENGINEERING

Vol. 18    No. 6    December 2008

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Purification and enzymatic characteristics of cysteine desulfurase, IscS, in Acidithiobacillus ferrooxidans ATCC 23270
WU An-na(吴安娜), ZHANG Yan-fei(张燕飞), ZHENG Chun-li(郑春丽), DAI Yun-jie(戴云杰),LIU Yuan-dong(刘元东), ZENG Jia(曾 嘉), GU Guo-hua(顾帼华), LIU Jian-she(柳建设)

Key Laboratory of Biometallurgy of Ministry of Education, School of Minerals Processing and Bioengineering,
Central South University, Changsha 410083, China

Abstract:A cysteine desulfurase protein, IscS, was encoded by the operon iscSUA in Acidithiobacillus ferrooxidans. The gene of IscS from Acidithiobacillus ferrooxidans ATCC 23270 was cloned and expressed in Escherichia coli. The protein was purified by one-step affinity chromatography to homogeneity. The final protein yield after affinity chromatography was 12.9%. The enzyme was characterized for thermal stability, pH and kinetic parameters. The molecular mass of recombinant IscS was 46 ku by SDS-PAGE. The optimum pH was 8.0−8.5. The enzyme had a temperature optimum at 30 ℃ and was relatively stable at 40 ℃, with 67% loss of activity. 1,5-I-AEDANS significantly inhibited IscS activity. Kinetic parameters Km and Vmax were found to be 0.11 mmol/L and 2.57 μmol/(L∙min).

 

Key words: Acidithiobacillus ferrooxidans; IscS; purification; optimum pH; optimum temperature; inhibition; kinetics

ISSN 1672-7029
CN 43-1423/U

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