Mathematical Modeling Thermal Stability Activity Inulinase Enzyme Reaction Biology Essay




The method was based on mathematical modeling of the thermal stability and activity of the enzyme and was developed using thermodynamic concepts and experimental data from free and immobilized. In modeling the thermal stability and activity of inulinase Santos et al. used a concept based on taking into account the effects of time and temperature on the enzymatic process. In this concept, kinetic parameters are related to the reaction rate at a fixed time of measurement, although due to enzyme deactivation a gradual decrease in enzyme sequence occurs. Understanding the complex relationships between enzyme sequence, folding stability and catalytic activity is essential for applications, but current technologies cannot do that. solve both at the same time. Abstract. Inulinases are industrial food enzymes that have received a lot of attention recently. Inulin and inulin-containing materials are durable, economical polymeric carbohydrates that are readily hydrolyzed by microbial inulinases to fructose, glucose, and inulo-oligosaccharides. The inulinase gene can also be cloned. A plot of relative activity at zero time versus temperature. Fig. 3 illustrates that all five enzymes exhibit a true temperature optimum of catalytic activity as defined by the Equilibrium Model and that the values ​​of T opt are essentially in agreement with the established values ​​of T eq Table I. For β-lactamase and adenosine deaminase the,





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