S F De Cordt

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Three different alpha-amylases from Bacillus subtilis, B. amyloliquefaciens, and B. licheniformis, were mutually compared with respect to thermal stability, pressure stability, and combined pressure-temperature stability. Measurements of residual enzyme activity and residual denaturation enthalpy showed that the alpha-amylase from B. licheniformis has by(More)
In view of a possible application of the alpha-amylase from Bacillus licheniformis as a time-temperature integrator for evaluation of heat processes,(11) thermal inactivation kinetics of the dissolved and covalently immobilized enzyme were studied in the temperature range 90-108 degrees C. The D-values (95 degrees C) for inactivation of alpha-amylase,(More)
For the immobilization of Bacillus licheniformis alpha-amylase to porous glass beads, the performances of three possible linking agents, glutaric dialdehyde, benzoquinone and s-trichlorotriazine were assessed in respect of the protein yield, the enzymic activity and the thermostability of the immobilized enzyme. These three properties are to be evaluated in(More)
Differential scanning calorimetry (DSC) was used as a tool for rapid assay of the thermostability of two Bacillus sp. alpha-amylases and horseradish peroxidase as a function of the concentration of glycerol, sorbitol, and sucrose. In this screening study, the DSC peak temperature proved to be a good measure of protein thermostability. By means of isothermal(More)
In this review, current methods used to evaluate the integrated impact of time and temperature upon preserving a food product by a heat treatment are considered. After identifying the basic premise any preservation scheme shall meet, the central role of a feasible description for the heat activation kinetics of microorganisms, their spores, and other(More)
The influence of polyhydric alcohols and carbohydrates on the thermostability, i.e., the heat inactivation kinetics, of Bacillus licheniformis alpha-amylase was studied in the temperature range 96 degrees to 130 degrees C. High concentrations (from 9 to 60 weight percent) of glycerol, sorbitol, mannitol, sucrose, or starch can markedly decrease the(More)
Thermal inactivation kinetics of Bacillus subtilis alpha-amylase (BSA) in different environmental conditions was studied by performing isothermal experiments. As a response property, residual enzymic activity and residual heat of enzyme deterioration were chosen. A comparison of processing values determined from the read-out of a system with actual(More)
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