Purification, characterization, thermal, and high-pressure inactivation of pectin methylesterase from bananas (cv Cavendish)
Related Experiment Video
Updated: Oct 1, 2026

Isolation and Biophysical Study of Fruit Cuticles
Published on: March 30, 2012
B Ly Nguyen1, A Van Loey, D Fachin
1Laboratory of Food Technology, Department of Food and Microbial Technology, Faculty of Agricultural and Applied Biological Sciences, Katholieke Universiteit Leuven, Kasteelpark Arenberg 22, B-3001 Heverlee (Leuven), Belgium.
Abstract:
Pectin methylesterase (PME) was extracted from bananas (cv Cavendish) and purified by affinity chromatography on a CNBr-Sepharose-PME inhibitor (PMEI) column. A single protein and PME activity peak was obtained. For banana PME, a biochemical characterization in terms of molar mass (MM), pI, and kinetic parameters was performed. In a second step, the thermal and high-pressure stability of the enzyme was studied. Isothermal inactivation of purified banana PME could be described by a first-order kinetic model in a temperature range of 65 degrees to 72.5 degrees C, whereas its isobaric-isothermal inactivation followed a fractional-conversion model. Banana PME was found to be more thermally stable compared with PMEs extracted from orange, tomato, and apple.
