TY - JOUR
T1 - Effect of heat and thermosonication treatments on peroxidase inactivation kinetics in watercress (Nasturtium officinale)
AU - Cruz, Rui M. S.
AU - Vieira, Margarida C.
AU - Silva, Cristina L. M.
PY - 2006/1/1
Y1 - 2006/1/1
N2 - The effect of heat and the combined heat/ultrasound (thermosonication) treatment on the inactivation kinetics of peroxidase in watercress (Nasturtium officinale) was studied in the temperature range of 40-92.5 °C. In the heat blanching processes, the enzyme kinetics showed a first-order biphasic inactivation model. The activation energies and the rates of the reaction at a reference temperature for both the heat-labile and heat-resistant fractions were, respectively, Ea1 = 421 ± 115 kJ mol-1 and Ea2 = 352 ± 81 kJ mol-1, k184.6°C= 18±14min-1 and k284.6°C=0.24±0.14min-1. The initial relative specific activity for both isoenzyme fractions were also estimated, being C 01 = 0.5 ± 0.08 μmol min-1 mg protein -1 and C02 = 0.5 ± 0.06 μmol min-1 mg protein-1, respectively. The application of thermosonication was studied to enable less severe thermal treatments and, therefore, improving the quality of the blanched product. In this treatment the enzyme kinetics showed a first-order model. The activation energy, the rate of reaction at a reference temperature and the initial relative specific activity were, respectively, Ea3 = 496 ± 65 kJ mol-1, k387.5°C= 10±2min-1 and C03 = 1 ± 0.05 μmol min-1 mg protein-1, proving that the enzyme became more heat labile. The present findings will help to design the blanching conditions for the production of a new and healthy frozen product, watercress (Nasturtium officinale), with minimized colour or flavour changes along its shelf life.
AB - The effect of heat and the combined heat/ultrasound (thermosonication) treatment on the inactivation kinetics of peroxidase in watercress (Nasturtium officinale) was studied in the temperature range of 40-92.5 °C. In the heat blanching processes, the enzyme kinetics showed a first-order biphasic inactivation model. The activation energies and the rates of the reaction at a reference temperature for both the heat-labile and heat-resistant fractions were, respectively, Ea1 = 421 ± 115 kJ mol-1 and Ea2 = 352 ± 81 kJ mol-1, k184.6°C= 18±14min-1 and k284.6°C=0.24±0.14min-1. The initial relative specific activity for both isoenzyme fractions were also estimated, being C 01 = 0.5 ± 0.08 μmol min-1 mg protein -1 and C02 = 0.5 ± 0.06 μmol min-1 mg protein-1, respectively. The application of thermosonication was studied to enable less severe thermal treatments and, therefore, improving the quality of the blanched product. In this treatment the enzyme kinetics showed a first-order model. The activation energy, the rate of reaction at a reference temperature and the initial relative specific activity were, respectively, Ea3 = 496 ± 65 kJ mol-1, k387.5°C= 10±2min-1 and C03 = 1 ± 0.05 μmol min-1 mg protein-1, proving that the enzyme became more heat labile. The present findings will help to design the blanching conditions for the production of a new and healthy frozen product, watercress (Nasturtium officinale), with minimized colour or flavour changes along its shelf life.
KW - Heat
KW - Inactivation
KW - Kinetics
KW - Modelling
KW - Peroxidase
KW - Ultrasound
KW - Watercress (Nasturtium officinale)
UR - http://www.scopus.com/inward/record.url?scp=22544459639&partnerID=8YFLogxK
U2 - 10.1016/j.jfoodeng.2004.11.007
DO - 10.1016/j.jfoodeng.2004.11.007
M3 - Article
AN - SCOPUS:22544459639
SN - 0260-8774
VL - 72
SP - 8
EP - 15
JO - Journal of Food Engineering
JF - Journal of Food Engineering
IS - 1
ER -