Kinetics and Thermodynamics of Thermal Inactivation of β-Galactosidase from Aspergillus oryzae

Klein, Manuela Poletto; Sant’Ana, Voltaire; Hertz, Plinho Francisco; Rodrigues, Rafael C.; Ninow, Jorge Luiz

doi:10.1590/1678-4324-2018160489

Cited by 10 publications

(7 citation statements)

References 40 publications

(42 reference statements)

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“…The degree and/or intensity of the thermal disruption of the noncovalent linkages in enzymes can be predicted through analysis of the enthalpy parameter, ΔH # [ 62 , 71 ]. It can be seen from Table 4 that while ΔG # increased with increasing temperature, ΔH # , like ΔS # , remained unchanged for each lipase.…”

Section: Resultsmentioning

confidence: 99%

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

Ortega

Sáez

Palacios

et al. 2022

IJMS

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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.

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Section: Resultsmentioning

confidence: 99%

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

Ortega

Sáez

Palacios

et al. 2022

IJMS

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“…The 3D plot with a determination coefficient of R 2 = 0.977 is shown in Figure 2. As already mentioned (Klein et al, 2018), this representation is an innovative approach in the field of thermal inactivation of enzymes, offering the possibility to evaluate the interaction of time and temperature on enzyme activity. For a better analyze of the thermal stability of Rpbgal, EM parameters are used to plot activity versus time (Figure 3).…”

Section: Resultsmentioning

confidence: 99%

“…In order to assess the possibilities that Rpbgal could offer in food processing industries from the thermal properties point of view, it is compared to a commercial βgalactosidase from Aspergillus oryzae. Recently, the thermal inactivation of this enzyme (CAS Number: 9031-11-2) was studied by Klein et al (2018) in the temperature range 331 -339 K using oNPG as substrate in an acidic buffer. The temperature dependence of tR obtained for Rpbgal is compared with that of the commercial βgalactosidase in Figure 4.…”

Section: Resultsmentioning

confidence: 99%

Modeling of the thermal behaviour of free β-galactosidase from palm weevil, Rhynchophorus palmarum Linn. (Coleoptera: Curculionidae) larvae using Equilibrium model

Kambiré¹,

Gnanwa²,

Boa³

et al. 2022

Int. J. Bio. Chem. Sci

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β-galactosidases are a class of enzyme widely used as biocatalysts in the food, dairy, and fermentation industries. However, due to their biological origin, enhancement of these enzymes is generally necessary. The effect of temperature upon enzymes is a mandatory stage in rational enzyme engineering. The present work was devoted to Rhynchophorus palmarum Linn. β-galactosidase (Rpbgal) as part of the investigation of insect-derived enzymes for biotechnological applications. The thermal behaviour of Rpbgal has been studied in the temperature range 303-353 K by measuring enzymatic activities in presence of oNPG as substrate. Equilibrium model which gives complete and quantitative description of the effect of temperature on enzyme activity has been used to analyze experimental data. A satisfactorily agreement between the calculated results and the experimental data was obtained. The thermodynamic parameters provided by this model were given. Results showed that Rpbgal is relatively stable and active at 323 K. Temperatures over 330 K produce a significant decrease in the enzyme activity. In the temperature range 331 - 339 K, Rpbgal showed the best thermal stability compared to a commercial β-galactosidase from Aspergillus oryzae.

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“…Inactivation is to be a process where the secondary, tertiary or quaternary structure of a protein changes without breaking covalent bonds [47] Therefore, the plots of residual activity vs. incubation time for the enzyme were linear, with R2 > 81 %, this was indicating that the inactivation could be expressed in terms of rst order kinetics in the temperature range of 50-65°C. The kinetic enzymatic modelling of thermal inactivation, and the determination of its thermodynamic parameters were analyzed at changeable temperatures and various conditions by [48].…”

Section: Discussionmentioning

confidence: 99%

Antioxidant and beta-Galactosidase Inhibitory Studies of Methanolic Extract of Juniperus Phoenicea and Calicotome Villosa from Jordan

Al-Mustafa

Al-Tawarah

Al-Sheraideh

et al. 2021

Preprint

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Background: We investigated Juniperus Phoenicea (J. Phoenicea) and Calicotome Villosa (C. Villosa) from Jordan for phenolic contents, antioxidant, anti β-Galactosidase activities, in an attempt to rationalize its use in lactose metabolism disorders. The kinetic parameters of leave extracts, galactose, glucose, fructose and acarbose were evaluated. Also, the thermodynamic parameters of the enzyme thermal inactivation were determined. Methods: JP and cv crude methanolic extracts were evaluated for 1,1-diphenyl,2-picrylhydrazyl (DPPH) free radical scavenging activity and ferric reducing antioxidant power (FRAP). Further, β-Galactosidase inhibitory activities were performed using O-nitrophenyl-beta-D-galactopyranoside as substrate. Moreover, total phenolic contents, flavonoids and flavonols of plants extracts were determined and expressed in mg of gallic acid equivalent (mg GAE/g dry extract) or rutin equivalent per gram of dry extract (mg RE/g dry extract).Results: Phytochemical screening of the crude extract of J. Phoenicea and C. Villosa leaves contained phenols, alkaloids, flavonoids, terpenoids, anthraquinones and glycosides. J. Phoenicea exhibited high flavonoids and flavonols contents than C. Villosa but both J. Phoenicea and C. Villosa contained high phenolic and showed concentration dependent DPPH scavenging activity, with J. Phoenicea (IC50 =11.1 μg/ml), C. Villosa (IC50 =15.6 μg/ml), respectively. According to FRAP assay, the antioxidant power activity of plants extracts was concentrations dependent. The β-galactosidase % inhibition was increased as the concentration of of J. phoenicea, C. villosa and rutin increased. The mode of inhibition of β-galactosidase by J. phoenicea (IC50= 65 µg/ml) and C. villosa (IC50= 700 µg/ml) extracts was non-competitive and mixed-inhibition, respectively. Also, rutin was affected in a competitive (IC50 = 75 µg/ml) inhibition. β-galactosidase half-life was 108 min at 55°C, thermodynamic parameters revealed an activation energy of 208.88 kJ mol-1 and the inactivation kinetic follows a first-order reaction with k-values ranges between 0.0862 and 0.0023 min-1. The enzyme showing a decreasing trend of enthalpy of denaturation (∆H°) as temperature increase but value of free energy of thermal denaturation (∆G°) for β-galactosidase was decreased with increasing in temperature. The calculated entropy of inactivation (∆S°) at each temperature showed positive values, which means there are no significant processes of aggregation.Conclusions: J.phoenicea and C.villosa have inhibiting effect on β-galactosidase activity. Thermodynamic approach shows an enzyme stable and suggests that inactivation mechanism is based on molecular structural changes.

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Kinetics and Thermodynamics of Thermal Inactivation of β-Galactosidase from Aspergillus oryzae

Cited by 10 publications

References 40 publications

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

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

Modeling of the thermal behaviour of free β-galactosidase from palm weevil, Rhynchophorus palmarum Linn. (Coleoptera: Curculionidae) larvae using Equilibrium model

Antioxidant and beta-Galactosidase Inhibitory Studies of Methanolic Extract of Juniperus Phoenicea and Calicotome Villosa from Jordan

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