Kinetic parameters for the thermal inactivation of quality-related enzymes in carrots and potatoes.
Kinetic parameters for the thermal inactivation of several enzymes in carrot and potato homogenates have been determined. In carrots the most heat-resistant activity was polygalacturonase, followed by peroxidase and pectinmethylesterase. In potatoes peroxidase was the most resistant, followed by pectin methylesterase, polyphenol oxidase, and lipoxygenase. There were several notable similarities between the inactivation kinetics in the two vegetables. In both cases peroxidase activity gave simple first-order inactivation kinetics but yielded a curved Arrhenius plot for the temperature dependence. Pectin methylesterase in both commodities consisted of a labile and a resistant form. The relative amounts of the two forms and the temperature dependences for their inactivation were also similar.
Anthon
Gordon E
GE
Department of Food Science and Technology, University of California, Davis, California 95616, USA. geanthon@ucdavis.edu
Barrett
Diane M
DM
D002265:Carboxylic Ester Hydrolases / Q000378:metabolism; D004156:Catechol Oxidase / Q000378:metabolism; D018552:Daucus carota / Q000201:enzymology*; D004795:Enzyme Stability; D006358:Hot Temperature; D007700:Kinetics; D008084:Lipoxygenase / Q000378:metabolism; D009195:Peroxidase / Q000378:metabolism; D011096:Polygalacturonase / Q000378:metabolism; D011198:Solanum tuberosum / Q000201:enzymology*; D013816:Thermodynamics
D004156:Catechol Oxidase; D009195:Peroxidase; D008084:Lipoxygenase; D002265:Carboxylic Ester Hydrolases; C022323:pectinesterase; D011096:Polygalacturonase