Thermostability conditions and catalytic characterization of isocitrate dehydrogenase from Bacillus licheniformis

• Authors: P. Zabielski
• Languages of publication: PL

Abstracts

EN

The NADP+ - dependent isocitrate dehydrogenase (IDH) from Bacillus licheniformis was partially purified using ammonium sulphate fractionation and gel filtration on Sephadex G-200 column. The enzyme preparation had specific activity of 1.52 U mg-1. The temperature optimum for the IDH activity was about 59C. The Arrthenius activation energy was determined to be 65.3 kJ/mol below 47C, and 18.3 kJ/mol above this temperature. The IDH activity at 65C was much protected by isocitrate and magnesium, but no NADP+. Manganese ions were more efficient activators of the enzyme than Mg2+. Calcium ions rather inhibited the IDH. The Km values for DL-isocitrate and NADP+ in phosphate buffer (pH 7.4) at 20C were 85.5 and 4.9 muM, respectively; at 58C the corresponding values were 181.5 and 69.3 muM.

Keywords

EN

BACILLUS LICHENIFORMIS; CATALYTIC PROPERTY; ISOCITRATE DEHYDROGENASE; THERMOSTABILITY

Discipline

• BIOTECHNOLOGY: BIOTECHNOLOGY

• Publisher: Committee of Biotechnology, Polish Academy of Sciences
• Journal: Biotechnologia
• Year: 2001
• Issue: 3
• Pages: 219-230

Contributors

author

P. Zabielski

• Document Type: ARTICLE
• Publication order reference: P. Zabielski, Instytut Biologii, Uniwersytet w Bialymstoku, ul. Swierkowa 20B, 15-950 Bialystok, Poland