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Title: Kinetic study of the irreversible thermal and pressure inactivation of myrosinase from broccoli (Brassica oleracea L-Cv. Italica)
Authors: Ludikhuyze, Linda ×
Ooms, V
Weemaes, C
Hendrickx, Marc #
Issue Date: Jan-1999
Publisher: Amer chemical soc
Series Title: Journal of Agricultural and Food Chemistry vol:47 issue:5 pages:1794-1800
Abstract: Thermal and pressure inactivation of myrosinase from broccoli was kinetically investigated. Thermal inactivation proceeded in the temperature range 300-60 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.
URI: 
ISSN: 0021-8561
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Centre for Food and Microbial Technology
× corresponding author
# (joint) last author

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