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Title: Purification and thermal and high-pressure inactivation of pectinmethylesterase isoenzymes from tomatoes (Lycopersicon esculentum): A novel pressure labile isoenzyme
Authors: Plaza Fraile, Lucia ×
Duvetter, Thomas
Monfort, Silvia
Clynen, Elke
Schoofs, Liliane
Van Loey, Ann
Hendrickx, Marc #
Issue Date: Oct-2007
Publisher: Amer chemical soc
Series Title: Journal of Agricultural and Food Chemistry vol:55 issue:22 pages:9259-9265
Abstract: Tomato pectin methylesterase (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 degrees C, whereas for the thermolabile isoenzyme, temperatures at around 60 degrees 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 degrees 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 degrees C or 650 MPa and 40 degrees C. Inactivation kinetics at pH 6.0 could be accurately described by a first-order model.
ISSN: 0021-8561
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Animal Physiology and Neurobiology Section - miscellaneous
Centre for Food and Microbial Technology
× corresponding author
# (joint) last author

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