期刊
APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
卷 177, 期 1, 页码 217-225出版社
HUMANA PRESS INC
DOI: 10.1007/s12010-015-1739-3
关键词
Oceanimonas smirnovii; Phosphoenolpyruvate carboxylase; Characterization; Bicarbonate
资金
- Basic Core Technology Development Program for the Oceans
- Polar Regions of the National Research Foundation (NRF) - Ministry of Science, ICT and Future Planning [NRF-2010-0020501]
In this study, phosphoenolpyruvate carboxylase (PEPC) derived from Oceanimonas smirnovii (OS) was expressed as a soluble protein in Escherichia coli BL21(DE3). We isolated OS-PEPC (a recombinant PEPC protein) by his-tag purification. The purified protein showed a single band upon analysis with SDS-PAGE, and it had an apparent molecular mass of 98 kDa. Pufied OS-PEPC showed a specific activity value of 21.8 +/- A 0.495 U/mg protein. Especially, OS-PEPC showed the enzymatic activity between 40 and 50 A degrees C. It maintained enzymatic activity in basic pH conditions (pH value, 9-10). We also measured OS-PEPC PEP and HCO3 (-) saturation kinetics and confirmed the effect of divalent cation on OS-PEPC activity.
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