The present study evaluated the kinetics and thermodynamic parameters for the thermal inactivation of inulinase. The thermoinactivation behaviours of inulinase under 40, 50, 60 and 70°C were observed. Residue activity of inulinase after incubated for a certain time under the tested temperatures, respectively. The inactivation rate constants (kin) of inulinase under different temperatures were c...

Salmonellosis outbreaks related to consumption of raw almonds have encouraged the scientific community to study the inactivation kinetics of pathogens in this dry commodity. However, the low moisture content of the product presents a challenge for thermal control, because the time required to achieve the desired thermal inactivation of microorganisms increases sharply with reduced moisture con...

Potassium ions, and to a less extent, ammonium, magnesium, and barium ions, protect streptolysin S against thermal inactivation.

1. The thermal inactivation time at 41.5 degrees C. of the H. F. and Frank strains of herpes simplex virus, under the conditions described, was 80 hours. 2. A strain of herpes virus recently recovered from a patient treated with a physically induced fever had a thermal inactivation time of 50 hours at 41.5 degrees C. 3. The neurotropic factor of the H. F. and Frank strains of virus was more res...

The effect of the lipid environment on the thermostability of three respiratory terminal oxidases was determined. Cytochrome-c oxidase from beef heart and Bacillus stearothermophilus were used as representative proteins from mesophilic and thermophilic origin, respectively. Quinol oxidase from the archaeon Sulfolobus acidocaldarius represented the model for a extreme thermoacidophilic enzyme. A...

The inactivation of naturally occurring bacterial indicators and bacteriophages by thermal treatment of a dewatered sludge and raw sewage was studied. The sludge was heated at 80 degrees C, and the sewage was heated at 60 degrees C. In both cases phages were significantly more resistant to thermal inactivation than bacterial indicators, with the exception of spores of sulfite-reducing clostridi...

Investigations were performed on the structural features responsible for kinetic thermal stability of a thermostable carboxypeptidase from the thermoacidophilic archaebacterium Sulfolobus solfataricus which had been purified previously and identified as a zinc metalloprotease [Colombo, D'Auria, Fusi, Zecca, Raia and Tortora (1992) Eur. J. Biochem. 206, 349-357]. Removal of Zn2+ by dialysis led ...

The study of heat inactivation is often of considerable value in the characterization of proteolytic enzymes. This is true because in most cases these proteases appear to be inactivated at different rates at the same temperature and pH values. Also the determination of the inactivation velocity constants at different temperatures makes it possible to evaluate the critical thermal increment of t...

The effect of pH on the thermal inactivation of staphylococcal enterotoxin A was investigated. Analysis of heated toxin by immunodiffusion in gel indicated that enterotoxin A in beef bouillon was inactivated faster at pH 5.3 than at pH 6.2. The z values (slopes) for the heat inactivation curves at pH 6.2 and 5.3 were 49.5 and 55 F (about 27 and 30 C), respectively. Enterotoxin produced and heat...

A rapid method is developed to analyze the kinetics of thermal inactivation of enzymes that exhibit a nonlinear biphasic log(activity)-time relationship. Thermal destruction experiments on alcohol dehydrogenase from baker's yeast demonstrate the applicability of the method. The method is based on physical considerations (as opposed to mathematical curve fitting/regression methods) and also serv...