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Abstract

The demand of energy and the search for alternative energy sources are the reason why scientists are interested in starch hydrolysis. The aim of the work was to experimental study of the hydrolysis of starch by α–amylase from porcine pancreas with α–amylase deactivation. Based on the experiments data, the parameters of starch hydrolysis by α– amylase with deactivation of enzyme was estimated. A mathematical model of temperature impact on the activity of α–amylase from porcine pancreas was used. It has been estimated that the activation energy Ea and the deactivation energy Ed were equal to 66 ± 4 kJ/mol and 161 ± 12 kJ/mol, respectively. Additionally, specific constant of starch hydrolysis k 0 and specific constant of α–amylase deactivation k d0 were calculated. The optimum temperature Topt equal to 318 ± 0.5 K was obtained from mathematical model. The obtained values of Ea, Ed, k 0 and k d0 parameters were used to the model starch hydrolysis by α–amylase from porcine pancreas at 310 K and 333 K.
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Authors and Affiliations

Justyna Miłek
1
ORCID: ORCID
Ireneusz Grubecki
2
ORCID: ORCID
Wirginia Tomczak
1
ORCID: ORCID

  1. Bydgoszcz University of Science and Technology, Department of Chemical and Biochemical Engineering, Faculty of Chemical Technology and Engineering, Semianryjna 3, 85-326 Bydgoszcz, Poland
  2. Cracow University of Technology, Faculty of Chemical Engineering and Technology, Warszawska 24, 31-155 Cracow, Poland
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Abstract

The paper presents a comparative analysis to determine the optimal temperatures and the activation energies for various origin endo-inulinases from Aspergillus niger. The parameters were estimated based on the literature of the activity curves vs. temperature for hydrolysis of inulin. It was assumed that both the hydrolysis reaction process and the deactivation process of endo-inulinase were first-order reactions by the enzyme concentration. A mathematical model describing the effect of temperature on endo-inulinases from Aspergillus niger activity was used. Based on the comparison analysis, values of the activation energies Ea were in the range from 23:53  3:20 kJ/mol to 50:66  3:61 kJ/mol, the deactivation energies Ed were in the range from 88:42  5:03 kJ/mol to 142:87  2:75 kJ/mol and the optimum temperatures Topt were obtained in the range from 317:12  0:83 K to 332:55  0:72 for endo-inulinase A. niger.

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Authors and Affiliations

Justyna Miłek
ORCID: ORCID

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