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 12 publications

(7 citation statements)

References 40 publications

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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

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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 plots of residual activity vs. incubation time for the enzyme were linear, with R 2 > 81%, which indicated that the inactivation could be expressed in terms of first-order kinetics in the temperature range of 50–65 °C. The kinetic enzymatic modeling of thermal inactivation and the determination of its thermodynamic parameters were analyzed at changeable temperatures and various conditions by [ 66 ]. The determinations of half-life (t 1/2 ) are more accurate and reliable especially when computing the stability properties of an enzyme at different temperatures [ 67 ].…”

Section: Discussionmentioning

confidence: 99%

Phytochemical analysis, antioxidant and in vitro β-galactosidase inhibition activities of Juniperus phoenicea and Calicotome villosa methanolic extracts

et al. 2021

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Background Juniperus Phoenicea (JP) and Calicotome Villosa (CV) are used by Jordanian populations as herbal remedies in traditional medicine. Herein, the phytochemical contents of their methanolic extracts were analyzed and their antioxidant as well as in vitro anti- β-Galactosidase activities were evaluated; their effect on β-Galactosidase enzyme kinetics was evaluated and the thermodynamic of the enzyme was determined. Methods The antioxidant activity of JP and CV crude methanolic extracts was evaluated using 1,1-diphenyl,2-picrylhydrazyl (DPPH) free radical scavenging and ferric reducing antioxidant power (FRAP) assays; however, the effect of the plants’ crude extracts on β-Galactosidase activity and kinetics was evaluated in vitro. Moreover, total phenolic, flavonoids, and flavonols content in plants’ extracts were determined and expressed in Gallic acid equivalent (mg GAE/g dry extract) or rutin equivalent (mg RE/g dry extract). Results Phytochemical screening of the crude extracts of JP and CV leaves revealed the presence of phenols, alkaloids, flavonoids, terpenoids, anthraquinones, and glycosides. Flavonoids and flavonols contents were significantly higher in JP than in CV (p < 0.05). Furthermore, an analogous phenolic content was detected in both JP and CV methanolic extracts (103.6 vs 99.1 mg GAE/g extract). The ability of JP extract to scavenge DPPH radicals was significantly higher than that of CV extract with IC50 = 11.1 μg/ml and 15.6 μg/ml, respectively. However, their extracts revealed relatively similar antioxidant capacities in FRAP assay; their activity was concentration dependent. The JP extract inhibited β—galactosidase enzyme activity with a significant IC50 value compared to CV extract; they exhibited their inhibitory activities at IC50 values 65 µg/ml and 700 µg/ml, respectively. Rutin revealed anti-β-galactosidase activity at IC50 = 75 µg/ml. The mode of inhibition of β-galactosidase by JP, CV, and rutin was non-competitive, mixed, and competitive inhibition, respectively. Thermodynamic and enzyme inactivation kinetics revealed that β-galactosidase has a half-life time of 108 min at 55 °C, activation energy of 208.88 kJ mol−1 and the inactivation kinetics follows a first-order reaction with k-values 0.0023–0.0862 min−1 and positive entropy of inactivation (∆S°) values at various temperatures, indicating non-significant processes of aggregation. Conclusions The methanolic extracts of JP and CV possess anti-hyperglycemic and antioxidant activities with potential pharmaceutical applications.

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

Cited by 12 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

Phytochemical analysis, antioxidant and in vitro β-galactosidase inhibition activities of Juniperus phoenicea and Calicotome villosa methanolic extracts

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

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