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| Title
| - Purification and Thermal and High-Pressure Inactivation of Pectinmethylesterase Isoenzymes from Tomatoes (Lycopersicon esculentum): A Novel Pressure Labile Isoenzyme
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| Abstract
| - Tomato pectinmethylesterase (PME) was successfully purified by a two-step method consisting of affinity chromatography followed by cation exchange chromatography. According to this procedure, four different isoenzymes were identified representing molar masses around 34.5-35.0 kDa. Thermal and high-pressure inactivation kinetics of the two major isoenzymes of tomato PME were studied. A striking difference between their process stability was found. The thermostable isoenzyme was completely inactivated after 5.0 min at 70 °C, whereas for the thermolabile isoenzyme, temperatures at around 60 °C were sufficient for complete inactivation. The thermostable isoenzyme was also found to be pressure stable since no inactivation was observed after 5.0 min of treatment at 800 MPa and 20 or 40 °C. The thermolabile isoenzyme appeared to be pressure labile since it could be completely inactivated after 5.0 min of treatment at 700 MPa and 20 °C or 650 MPa and 40 °C. Inactivation kinetics at pH 6.0 could be accurately described by a first-order model.
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| Alternative Title
| - Purification and Inactivation of Pectinmethylesterase Isoenzymes
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