Kinetic Modeling, Thermodynamic Approach and Molecular Dynamics Simulation of Thermal Inactivation of Lipases from Burkholderia cepacia and Rhizomucor miehei

Abstract

The behavior against temperature and thermal stability of enzymes is a topic of importance for industrial biocatalysis. This study focuses on the kinetics and thermodynamics of the thermal inactivation of Lipase PS from B. cepacia and Palatase from R. miehei. Thermal inactivation was investigated using eight inactivation models at a temperature range of 40–70 °C. Kinetic modeling showed that the first-order model and Weibull distribution were the best equations to describe the residual activity of Lipase PS and Palatase, respectively. The results obtained from the kinetic parameters, decimal reduction time (D and tR), and temperature required (z and z’) indicated a higher thermal stability of Lipase PS compared to Palatase. The activation energy values (Ea) also indicated that higher energy was required to denature bacterial (34.8 kJ mol−1) than fungal (23.3 kJ mol−1) lipase. The thermodynamic inactivation parameters, Gibbs free energy (DG#), entropy (DS#), and enthalpy (DH#) were also determined. The results showed a DG# for Palatase (86.0–92.1 kJ mol−1) lower than for Lipase PS (98.6–104.9 kJ mol−1), and a negative entropic and positive enthalpic contribution for both lipases. A comparative molecular dynamics simulation and structural analysis at 40 °C and 70 °C were also performed.

Ethyl ester production with immobilized lipase in tin modified SBA‐15: Effect of the support characteristic and reaction conditions

“…As mentioned, the higher temperatures can cause deactivation of lipases, and the longer the lipases remain at high temperatures, the more impaired their performance will be. [ 57 ]…”

“…As mentioned, the higher temperatures can cause deactivation of lipases, and the longer the lipases remain at high temperatures, the more impaired their performance will be. [57] The optimal temperature for Burkholderia cepacia lipase in biodiesel production may vary according to the reaction medium condition. For instance, Abdulla and Ravindra [58] and You et al [59] reported an optimal temperature of 35 C. On the other hand, Li et al [60] found that the highest ester yield was achieved at 45 C. Overall, the optimal temperature for lipase performance depends on various parameters such as the alcohol-to-oil molar ratio, the immobilization technique, support nature, and enzyme thermostability.…”

Purification and characterization of L-arginine deiminase from Penicillium chrysogenum

“…The half-life (t 0.5 ) was calculated from a plot of the residual activity vs. the time and the deactivation rate constants (K d ) were estimated using the equation: t 0.5 = Ln (2)/ K d [ 27 ]. Half-life (t 0.5 ) is the required time for a reduction of 50% of the initial ADI activity at a particular temperature [ 28 ]. The D value was calculated using the equation: D = Ln (10)/ K d [ 27 ].…”

“…The Z value was calculated from the slope of the graph between Log D versus T (°C) using the equation: Slope = -1/ Z [ 27 ]. The Z-value indicates how many degrees of temperature are required for decimal reduction time to be tenfold higher or lower [ 28 ].…”

Purification, Biochemical and Kinetic Characterization of a Novel Alkaline sn-1,3-Regioselective Triacylglycerol Lipase from Penicilliumcrustosum Thom Strain P22 Isolated from Moroccan Olive Mill Wastewater

“…Owing to their broad spectrum of catalytic reactions, lipases are used in several industrial applications, such as detergent formulations, biodiesel synthesis, the production of pharmaceutical and cosmetic esters, food, and wastewater treatment [ 10 , 11 , 12 ]. Lipases are ubiquitous in nature and can be produced by a variety of plants, animals, and microorganisms [ 13 ]. However, microbial lipases are the most commercially useful for their indisputable role among biocatalysts [ 14 ].…”