The inulin hydrolysis by recombinant exo-inulinases: determination the optimum temperatures and activation energies

Abstract

The advantages of recombinant enzymes over native include the control in a production environment, product purity and also high yield. The paper presents the determination the optimum temperatures and the activation energies for various origin recombinant exo-inulinases, among others from Aspergillus niger, A. awamori, Kluyveromyces marxianus and K. cicerisporus. The parameters were estimated based on the literature of the activity curves versus temperature for hydrolysis of inulin. It was assumed that both the hydrolysis reaction process and the deactivation process of recombinant exo-inulinase were first-order reactions by the enzyme concentration. A mathematical model describing the effect of temperature on recombinant exo-inulinase activity was used. Based on the comparison analysis, values of the activation energies $${E_{\rm a }}$$ E a were in the range from $${32.01 \pm 7.80}$$ 32.01 ± 7.80 to $${43.83 \pm 4.87}$$ 43.83 ± 4.87 kJ mol$$^{-1}$$ - 1 , the deactivation energies $${E_{\rm d }}$$ E d were in the range from $${83.93 \pm 4.82}$$ 83.93 ± 4.82 to $${352.44 \pm 14.26}$$ 352.44 ± 14.26 kJ mol$$^{-1}$$ - 1 and the optimum temperature $${T_{\rm opt }}$$ T opt were obtained in the range from $${318.91 \pm }$$ 318.91 ± 1.19 to $${328.76 \pm 0.25}$$ 328.76 ± 0.25 K.

Production, Biochemical Characterization, and Kinetic/Thermodynamic Study of Inulinase from Aspergillus terreus URM4658

“…The very low value of the activation energy of inulin hydrolysis (19.59 ± 1.10 kJ mol −1 ) indicates that low energy is required to form the activated complex, which is an indicator of the high catalytic potential of this inulinase. It was lower than those of inulinases from other Aspergillus strains, such as A. niger (25.20–60.95 kJ mol −1 ) [ 30 ], A. welwitschiae MN056175 (21.82 kJ mol −1 ) [ 31 ], A. awamori (32.56 kJ mol −1 ) [ 32 ], and a marine strain of A. terreus (28.41 kJ mol −1 ) [ 33 ]. On the other hand, the relatively high value of standard enthalpy variation of enzyme unfolding equilibrium ( ∆H ° u ) (82.49 ± 1.10 kJ mol −1 ) highlights an unfavorable biocatalyst unfolding and then good performance of the process [ 16 ].…”

Study of starch hydrolysis by α–amylasefrom porcine pancreas with deactivation of enzyme

“…Equations ( 6)-( 8) were applied to determine the parameters Ea, Ed and Topt for inulin hydrolysis by recombinant exo-inulinase from Aspergillus niger (Miłek, 2022), endoinulinase from A. niger no recombinant (Miłek, 2020) and recombinant (Miłek, 2023), as well as for olive oil hydrolysis by lipase from porcine pancreas (Miłek, 2021b).…”

“…The software SigmaPlot 15.0 was used to estimate parameters occurring in Eq. ( 6) by nonlinear regression of Levenberg-Margurdt method already used in several previous studies Miłek (2021bMiłek ( , 2022Miłek ( , 2023.…”

The Energies of Activation and Deactivation of 2,4-Dichlorophenol Degradation by Horseradish Peroxidase Immobilized on the Modified Nanofibrous Membrane

“…Based on Equation ( 5), the parameters T opt , θ, and E d were estimated by the Levenberg-Marquardt procedure [17,[22][23][24][25][26] to calculate the minimum sum of squared errors (SSE).…”

“…The optimum temperatures and activation energies were determined for other bioprocesses by using enzymes. Processes such as inter alia starch hydrolysis by α-amylase from the porcine pancreas [25], inulin hydrolysis by recombinant exo-inulinases [26], and olive oil hydrolysis by porcine pancreas lipase [17] were analyzed.…”