Influence of pH on the Thermal Inactivation Kinetics of Horseradish Peroxidase in Aqueous Solution

LWT ◽  
2000 ◽  
Vol 33 (5) ◽  
pp. 362-368 ◽  
Author(s):  
Maria Adı́lia Lemos ◽  
Jorge C Oliveira ◽  
Jorge A Saraiva
2021 ◽  
Vol 2021 ◽  
pp. 1-7
Author(s):  
Evelyn ◽  
Chairul

Heat-resistant bacteria and molds can survive the pasteurization conditions used in high-acid fruit juices. The objective of this study was to evaluate the log reductions and thermal inactivation kinetics of spores of Bacillus subtilis bacteria and ascospores of Talaromyces flavus and Eupenicillium javanicum molds under influence of pH and sodium benzoate preservative. The spores were suspended in guava juice, processed at 90-100°C for B. subtilis and at 80-90°C for T. flavus and E. javanicum, and decimal reduction ( D ) values were estimated from the log survivor curves. Next, the effects of pH change (3.5-4.5) and 0.015% sodium benzoate addition on the D values of spores were investigated. Lower D values were obtained at higher temperatures ( D 100 ° C value of 2.32 min vs. D 90 ° C value of 15.33 min for B. subtilis, D 90 ° C value of 2.96 min vs. D 80 ° C value of 59.52 min for T. flavus, and D 90 ° C value of 1.58 min vs. D 80 ° C value of 21.32 min for E. javanicum). The D values decreased further (to 1.8 min at 100°C for B. subtilis, to 2.33 min at 90°C for T. flavus, and to 1.49 min at 90°C for E. javanicum) when the pH of guava juice was decreased from 4.1 to 3.5. Inclusion of sodium benzoate in pH 3.5 juice enhanced the thermal inactivation of spores ( D 100 ° C value decreased to 1.4 min for B. subtilis, to 1.98 min for T. flavus, and to 1.34 min for E. javanicum). To conclude, the combination of low pH and sodium benzoate provided the best method for spore inactivation, which could enhance food safety and extend food’s shelf life.


1988 ◽  
Vol 53 (3) ◽  
pp. 920-923 ◽  
Author(s):  
B.S. CHANG ◽  
K.H. PARK ◽  
D.B. LUND

1997 ◽  
Vol 60 (8) ◽  
pp. 967-972 ◽  
Author(s):  
CARMEN RODRIGO ◽  
ANDRÉS ALVARRUIZ ◽  
ANTONIO MARTÍNEZ ◽  
ANA FRÍGOLA ◽  
MIGUEL RODRIGO

The thermal inactivation kinetics of horseradish and asparagus peroxidase in high-temperature short-time conditions was studied by heating in a five-channel computer-controlled thermoresistometer. Horseradish peroxidase was heated between 111.5 and 145°C and the reaction was analyzed assuming that two isoenzymes with EaL = 44.1 and Eas = 22.0 kcal/mol were present. Asparagus peroxidase heated from 110 to l20°C reacted with first-order kinetics, with Ea = 20 kcal/mol. The five-channel computer-controlled thermoresistometer enabled us to study the inactivation kinetics of the more labile fraction of horseradish peroxidase at temperatures above 100°C; this equipment was suitable for studying the heat resistance of peroxidase at high temperatures.


2017 ◽  
Vol 40 (6) ◽  
pp. e12570 ◽  
Author(s):  
Maria F. Machado ◽  
Alexandra Sousa ◽  
Sónia M. Castro ◽  
Sílvia A. Moreira ◽  
Jorge A. Saraiva

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