Comparative study of the inactivation kinetics of pectinmethylesterase in tomato juice and purified form |
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| Authors: | Fachin Diana Van Loey Ann M Ly Nguyen Binh Verlent Isabel Indrawati Indrawati Hendrickx Marc E |
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| Institution: | Pontificia Universidade Católica do Paraná, Brazil, and Laboratory of Food Technology, Department of Food and Microbial Technology, Katholieke Universiteit Leuven, Kasteelpark Arenberg 22, B-3001 Leuven, Belgium. |
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| Abstract: | 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. |
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