A manganese catalase from Thermomicrobium roseum with peroxidase and catecholase activity
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- 作者：Robin Baginski ; Monika Sommerhalter
- 关键词：Thermomicrobium roseum ; Manganese catalase ; Catecholase ; Peroxidase ; Catalase ; phenol oxidase
- 刊名：Extremophiles
- 出版年：2017
- 出版时间：January 2017
- 年：2017
- 卷：21
- 期：1
- 页码：201-210
- 全文大小：
- 刊物类别：Biomedical and Life Sciences
- 刊物主题：Microbiology; Biotechnology; Biochemistry, general; Microbial Ecology;
- 出版者：Springer Japan
- ISSN：1433-4909
- 卷排序：21
文摘
An enzyme with catechol oxidase activity was identified in Thermomicrobium roseum extracts via solution assays and activity-stained SDS-PAGE. Yet, the genome of T. roseum does not harbor a catecholase gene. The enzyme was purified with two anion exchange chromatography steps and ultimately identified to be a manganese catalase with additional peroxidase and catecholase activity. Catalase activity (6280 ± 430 IU/mg) clearly dominated over pyrogallol peroxidase (231 ± 53 IU/mg) and catecholase (3.07 ± 0.56 IU/mg) activity as determined at 70 °C. Most enzyme kinetic properties were comparable to previously characterized manganese catalase enzymes. Catalase activity was highest at alkaline pH values and showed inhibition by excess substrate and chloride. The apparent Km and kcat values were 20 mM and 2.02 × 104 s−1 subunit−1 at 25 °C and pH 7.0.