4.7 Article

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

Journal

JOURNAL OF THERMAL ANALYSIS AND CALORIMETRY
Volume 148, Issue 3, Pages 859-866

Publisher

SPRINGER
DOI: 10.1007/s10973-022-11809-3

Keywords

Recombinant endo-inulinases; Activation energy; Deactivation energy; Optimum temperature

Ask authors/readers for more resources

The aim of this study was to determine the activation, deactivation energies, and optimum temperatures for recombinant endoinulinases from various origins. The activity of these enzymes at different temperatures was analyzed and a mathematical model was used to describe the temperature effect on enzyme activity. The results showed a range of values for activation energies, deactivation energies, and optimum temperatures for different sources of recombinant endoinulinases.
The aim of paper was to determine the activation, deactivation energies and optimum temperatures for recombinant endoinulinases 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 +/- 13.94 kJ mol(-1) to 62.62 +/- 17.24 kJ mol(-1) and in the range from 29.80 +/- 8.83 kJ mol(-1) to 92.69 +/- 15.31 kJ mol(-1) for recombinant endo-inulinase A. niger and various origins, respectively. The deactivation energies ED were from the range from 146.80 +/- 20.31 kJ mol(-1) to 301.95 +/- 95.81 kJ mol(-1) and in the range from 159.96 +/- 14.80 kJ mol(-1) to 289.43 +/- 21.18 kJ mol(-1) for recombinant endo-inulinase A. niger and various origins, respectively. The optimum temperatures Topt were obtained in the range from 328.67 +/- 1.32 K to 335.94 +/- 1.22 K and in the range from 319.41 +/- 0.85 K to 338.53 +/- 0.45 K for recombinant endo-inulinase A. niger and various origins, respectively.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.7
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available