Purification and partial characterization of Cu/Zn superoxide dismutase from Kluyveromyces marxianus

详细信息    查看全文

• 作者：Trayana Nedeva ; Pavlina Dolashka-Angelova ; Vesela Moshtanska ; Wolfgang Voelter ; Ventzislava Petrova ; Anna Kujumdzieva
• 关键词：Cu/Zn superoxide dismutase ; K. marxianus ; Purification ; Thermostability ; Glycoprotein
• 刊名：Journal of Chromatography B, Analytical Technologies in the Biomedical and Life Sciences
• 出版年：2009
• 出版时间：1 November 2009
• 年：2009
• 卷：877
• 期：29
• 页码：3529-3536
• 全文大小：766 K

文摘

A new thermostable Cu/Zn SOD from a thermotolerant yeast strain Kluyveromyces marxianus NBIMCC 1984 has been purified and characterized. The purification procedure comprises thermal treatment and dialysis, ion-exchange chromatography and chromatofocusing. The methodology is a rapid, efficient and highly specific, generating pure preparation (specific activity 996 U mg of protein⁻¹) with a yield of 53 % . The purified enzyme is a homodimer with Mw of 34 034 Da and has high N-terminal homology with other yeasts’ Cu/Zn SOD enzymes. The protein is characterized with some unique features such as—thermostability (t_1/2 at 70 °C = 30 min), pH stability in the alkaline range (7.5–8.5) and resistance to inhibitors and variety of chemicals. These characteristics reveal possibilities for wide practical application of K. marxianus Cu/Zn SOD enzyme.