Partial purification, characterization, and thermal and high-pressure inactivation of pectin methylesterase from carrots (Daucus carrota L.).
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.
Ly-Nguyen
Binh
B
Laboratory of Food Technology, Department of Food and Microbial Technology, Faculty of Agricultural and Applied Biological Sciences, Katholieke Universiteit Leuven, Kasteelpark Arenberg 22, B-3001 Leuven, Belgium.
Van Loey
Ann M
AM
Fachin
Diana
D
Verlent
Isabel
I
Indrawati
Indrawati
I
Hendrickx
Marc E
ME
D002265:Carboxylic Ester Hydrolases / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D002846:Chromatography, Affinity; D018552:Daucus carota / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D006358:Hot Temperature; D007525:Isoelectric Focusing; D007526:Isoelectric Point; D007700:Kinetics; D008970:Molecular Weight; D011312:Pressure
D002265:Carboxylic Ester Hydrolases; C022323:pectinesterase