Recombinant endo-inulinases: determination the activation and deactivation energies and optimum temperatures in inulin hydrolysis

Abstract

AbstractThe aim of paper was to determine the activation, deactivation energies and optimum temperatures for recombinant endo-inulinases of various origins, including also recombinant endo-inulinases from Aspergillus niger, Escherichia coli, Saccharomyces cerevisiae and Yarrowia lipolytica. The activity recombinant endo-inulinases of various origins vs. temperature curves were analyzed. A mathematical model describing the effect of temperature on recombinant endo-inulinase activity was used. Based on the analysis, values of the activation energies E were in the range from $${22.08 \pm 13.94}$$ 22.08 ± 13.94 kJ mol$$^{-1}$$ - 1 to $${62.62 \pm 17.24}$$ 62.62 ± 17.24 kJ mol$$^{-1}$$ - 1 and in the range from $${29.80 \pm 8.83}$$ 29.80 ± 8.83 kJ mol$$^{-1}$$ - 1 to $${92.69 \pm 15.31}$$ 92.69 ± 15.31 kJ mol$$^{-1}$$ - 1 for recombinant endo-inulinase A. niger and various origins, respectively. The deactivation energies $${E_{\mathrm{D}}}$$ E D were from the range from $${146.80 \pm 20.31}$$ 146.80 ± 20.31 kJ mol$$^{-1}$$ - 1 to $${301.95 \pm 95.81}$$ 301.95 ± 95.81 kJ mol$$^{-1}$$ - 1 and in the range from $${159.96 \pm 14.80}$$ 159.96 ± 14.80 kJ mol$$^{-1}$$ - 1 to $${289.43 \pm 21.18}$$ 289.43 ± 21.18 kJ mol$$^{-1}$$ - 1 for recombinant endo-inulinase A. niger and various origins, respectively. The optimum temperatures $${T_{\mathrm{opt}}}$$ T opt were obtained in the range from $${328.67 \pm 1.32}$$ 328.67 ± 1.32 K to $${335.94 \pm 1.22}$$ 335.94 ± 1.22 K and in the range from $${319.41 \pm 0.85}$$ 319.41 ± 0.85 K to $${338.53 \pm 0.45}$$ 338.53 ± 0.45 K for recombinant endo-inulinase A. niger and various origins, respectively.