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EN
For a long period of time the thermal processing has been considered as the only way to reduce the initial spore number of Alicyclobacillus acidoterrestris and prevent the spoilage of beverage especially the acidic one. The effect of temperature on the inactivation of bacterial spores is well documented. However is still not yet fully explored the interactions between the components of the tested environment. Alicyclobacillus acidoterrestris spores being resistant to the pasteurization treatment conditions normally applied to acidic fruit products can germinate and grow causing spoilage. Visual detection of spoilage is very difficult because Alicyclobacillus acidoterrestris does not produce gas during growth and incipient swelling of containers does not occur. Knowledge of the survival curves of Alicyclobacillus acidoterrestris spores suspended in natural and model environments is necessary to design pasteurization processes for high acidic fruit products. Therefore, this microorganism was suggested as the target to be used in the design of adequate pasteurization processes.
EN
Thermal stability of a-amylase in systems of different moisture content was investigated. Thermal inactivation kinetics could be accurately described by a first order model in all systems studied except the system of moisture content of 0.029 g H2O/g db showing a biphasic inactivation pattern. Heat stability of the enzyme was significantly increased in systems with reduced moisture content. In ail subsequent systems with reduced moisture content the heat stability of the enzyme was increased and reached maximum value at the lowest moisture content equal to 0.029 g H2O/g db.
EN
The study purpose was to determine the effect of temperature on stability of laccase from Cerrena unicolor. An attention was focused on elevated temperatures strongly influencing the enzyme stability in real process. It was stated that the four-parameter model of inactivation, related to the inactivation model by a series mechanism describes precisely the decay of enzyme activity.
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