No abstract

Pectin methylesterase (PME) was extracted from carrots and purified by affinity chromatography. The thermal high-pressure inactivation of the PME was investigated in a model system. Under these conditions, the (thermo) stable fraction is not inactivated and the isobaric-isothermal inactivation followed a fractional-conversion model. At lower pressures (< 300 MPa) and higher temperatures (> 50 °C), an antagonistic effect of pressure and heat was observed. A 2nd-and 3rd-degree polynomial model (derived from available thermodynamic model) was successfully used to describe the heat pressure dependence of the inactivation rate constants. From the purified carrot PME sample, the thermostable PME fraction was isolated. The thermal inactivation of this fraction followed first-order kinetics.

Pectinmethylesterase (PME) extracted from tomato fruit was purified by affinity chromatography. A single peak of PME activity was observed, presenting a molar mass of 33.6 kDa, an isoelectric point higher than 9.3, and an optimal temperature and pH for activity of 55 degrees C and 8.0, respectively. The processing stability of purified tomato PME in buffer solution was compared to PME stability in tomato juice. In both media, thermal inactivation of PME presented first-order inactivation kinetics, PME in tomato juice being more heat-labile than purified PME. Regarding high-pressure treatment, tomato PME showed to be very pressure-resistant, revealing an outspoken antagonistic effect of temperature and pressure. To avoid cloud loss in tomato juice, a time-temperature treatment of 1 min at 76.5 degrees C was calculated in order to have a residual PME activity of 1 x 10(-)(4) U/mL.

Pectin methylesterase (PME) from carrots (Daucus carrota L.) was extracted and purified by affinity chromatography on a CNBr-Sepharose 4B-PME inhibitor column. A single protein and PME activity peak was obtained. A biochemical characterization in terms of molar mass (MM), isoelectric points (pI), and kinetic parameters of carrot PME was performed. In a second step, the thermal and high-pressure stability of the enzyme was studied. Isothermal and combined isothermal-isobaric inactivation of purified carrot PME could be described by a fractional-conversion model.

Polygalacturonase (PG) was extracted from tomato fruit. The inactivation kinetics of the PG crude extract was investigated under isothermal and isobaric-isothermal conditions. Thermal inactivation of tomato PG in the temperature range 58 to 65 8C could be described by a fractional conversion model, and in the temperature range from 70 to 90 8C by a biphasic model. Pressure-temperature inactivation (range 300 to 600 MPa/5 to 50 8C) of tomato PG could be described by a fractional conversion model, which points to first-order inactivation kinetics of a pressure-sensitive enzyme fraction and to the occurrence of a pressure-stable PG fraction. A mathematical model describing the influence of pressure and temperature on the inactivation rate constant was formulated.