@misc{Zabielski_Piotr_Thermostability_2001, author={Zabielski, Piotr and Strumiło, Sławomir and Święcicka, Izabela}, volume={54}, number={3}, copyright={Creative Commons Attribution BY-SA 4.0 license}, journal={Biotechnologia, vol.54, 3 (2001)-.}, howpublished={online}, year={2001}, publisher={Committee on Biotechnology PAS}, publisher={Institute of Bioorganic Chemistry PAS}, language={pol}, abstract={The NADP+ - dependent isocitrate dehydrogenase (IDH) from Bacilluslicheniformis was partially purified using ammonium sulphate fractionation andgel filtration on Sephadex G-200 column. The enzyme preparation had specificactivity of 1.52 U mg ’. The temperature optimum for the IDH activity was about59°C. The Arrthenius activation energy was determined to be 65.3 kj/mol below47°C, and 18.3 kJ/mol above this temperature. The IDH activity at 65°C wasmuch protected by isocitrate and magnesium, but no NADP+. Manganese ionswere more efficient activators ofthe enzyme than Mg^+. Calcium ions rather inhibited the IDH. The Km values for DL-isocitrate and NADP+ in phosphate buffer(pH 7.4) at 20°C were 85.5 and 4.9 pM, respectively: at 58°C the correspondingvalues were 181.5 and 69.3 pM.}, type={Text}, title={Thermostability conditions and catalytic characterization of isocitratedehydrogenase from Bacillus licheniformis}, URL={http://rcin.org.pl/Content/138907/PDF/POZN271_174189_biotechnologia-2001-no3-zabielski.pdf}, keywords={biotechnology}, }