التفاصيل البيبلوغرافية
| العنوان: |
Production, Biochemical Characterization, and Kinetic/Thermodynamic Study of Inulinase from Aspergillus terreus URM4658. |
| المؤلفون: |
de Oliveira, Rodrigo Lira1 (AUTHOR), da Silva, Suzana Pedroza1 (AUTHOR), Converti, Attilio2 (AUTHOR) converti@unige.it, Porto, Tatiana Souza3 (AUTHOR) |
| المصدر: |
Molecules. Oct2022, Vol. 27 Issue 19, p6418. 15p. |
| مصطلحات موضوعية: |
*INULASE, *ASPERGILLUS terreus, *INULIN, *GIBBS' free energy, *SOLID-state fermentation, *WHEAT bran, *HYDROLYSIS |
| مستخلص: |
Inulinases are enzymes involved in the hydrolysis of inulin, which can be used in the food industry to produce high-fructose syrups and fructo-oligosaccharides. For this purpose, different Aspergillus strains and substrates were tested for inulinase production by solid-state fermentation, among which Aspergillus terreus URM4658 grown on wheat bran showed the highest activity (15.08 U mL−1). The inulinase produced by this strain exhibited optimum activity at 60 °C and pH 4.0. A detailed kinetic/thermodynamic study was performed on the inulin hydrolysis reaction and enzyme thermal inactivation. Inulinase was shown to have a high affinity for substrate evidenced by very-low Michaelis constant values (0.78–2.02 mM), which together with a low activation energy (19.59 kJ mol−1), indicates good enzyme catalytic potential. Moreover, its long half-life (t1/2 = 519.86 min) and very high D-value (1726.94 min) at 60 °C suggested great thermostability, which was confirmed by the thermodynamic parameters of its thermal denaturation, namely the activation energy of thermal denaturation (E*d = 182.18 kJ mol−1) and Gibbs free energy (106.18 ≤ ΔG*d ≤ 111.56 kJ mol−1). These results indicate that A. terreus URM4658 inulinase is a promising and efficient biocatalyst, which could be fruitfully exploited in long-term industrial applications. [ABSTRACT FROM AUTHOR] |
| قاعدة البيانات: |
Academic Search Index |
Full Text Finder