Journal of Agricultural and Food Chemistry vol:52 issue:18 pages:5724-5729
Pectin methylesterase (PME) from green bell peppers (Capsicum annuum) was extracted and purified by affinity chromatography on a CNBr-Sepharose-PMEI column. A single protein peak with pectin methylesterase activity was observed. For the pepper PME, a biochemical characterization in terms of molar mass (MM), isoelectric points (pI), and kinetic parameters for activity and thermostability was performed. The optimum pH for PME activity at 22 degreesC was 7.5, and its optimum temperature at neutral pH was between 52.5 and 55.0 degreesC. The purified pepper PME required the presence of 0.13 M NaCl for optimum activity. Isothermal inactivation of purified pepper PME in 20 mM Tris buffer (pH 7.5) could be described by a fractional conversion model for lower temperatures (55-57 degreesC) and a biphasic model for higher temperatures (58-70 degreesC). The enzyme showed a stable behavior toward high-pressure/temperature treatments.