Kinetic study of the irreversible thermal and pressure inactivation of myrosinase from broccoli (Brassica oleracea L. Cv. italica).
Thermal and pressure inactivation of myrosinase from broccoli was kinetically investigated. Thermal inactivation proceeded in the temperature range 30-60 degrees C. These results indicate that myrosinase is rather thermolabile, as compared to other food quality related enzymes such as polyphenol oxidase, lipoxygenase, pectinmethylesterase, and peroxidase. In addition, a consecutive step model was shown to be efficient in modeling the inactivation curves. Two possible inactivation mechanisms corresponding to the consecutive step model were postulated. Pressure inactivation at 20 degrees C occurred at pressures between 200 and 450 MPa. In addition to its thermal sensitivity, the enzyme likewise is rather pressure sensitive as compared to the above-mentioned food quality related enzymes. By analogy with thermal inactivation, a consecutive step model could adequately describe pressure inactivation curves. At 35 degrees C, pressure inactivation was studied in the range between 0. 1 and 450 MPa. Application of low pressure (<350 MPa) resulted in retardation of thermal inactivation, indicating an antagonistic or protective effect of low pressure.
Ludikhuyze
L
L
Department of Food and Microbial Technology, Faculty of Agricultural and Applied Biological Sciences, Katholieke Universiteit Leuven, Belgium.
Ooms
V
V
Weemaes
C
C
Hendrickx
M
M
D001937:Brassica / Q000201:enzymology*; D004795:Enzyme Stability; D006026:Glycoside Hydrolases / Q000037:antagonists & inhibitors / Q000737:chemistry*; D006358:Hot Temperature; D007700:Kinetics; D011312:Pressure; D013816:Thermodynamics
D006026:Glycoside Hydrolases; C022739:thioglucosidase