Kinetic and thermodynamic aspects of the process of thermal inactivition of kluyveromyces marxianus inulinase

Background: Inulinase is widely found in microorganisms and higher plants. It catalyzes the reaction of hydrolysis inulin, which present tubers roots many plants, to fructose a small amount glucose.
 Inulin one several plant-based polysaccharides that contain glucose or fructose. used as substrate industrial fermentation processes food industry due its relatively cheap abundant source for microbiological production high juices, ethanol, acetone butanol. Inulin-derived oligosaccharides are also medical sectors. produced from yeast K. marxianus at levels close commercial use. This indicates inulinase can be syrups. So our main object study effect different temperatures on conformation Kluyveromyces macromolecule, provide optimal conditions aniline by inulinase.
 Materials method: Method isolation purification enzyme marxianus, well determination protein content activity mentioned context research. Experiments were carried out thermal stability enzyme. For this, an solution concentration 5•10-5 mol / l was incubated time interval 10-60 min temperatures, followed catalytic activity.
 known types bonds interactions participate formation molecular structure enzymes, covalent bonds, hydrogen salt bridges, hydrophobic interactions, so goal molecule order hydrolysis. enzyme.
 Results: this revealed residual after 60 minutes incubation 50 °C 10% initial 7%. As Rate Constants inactivation 70 3.45.
 Conclusions: Results important useful determining parameters Based shape curves dependence temperature range 20-80 ° C.