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 Activity and Process Stability of Purified Green Pepper (Capsicum annuum) Pectin Methylesterase
Please use this identifier to cite or link to this item http://hdl.handle.net/10773/6973

title: Activity and Process Stability of Purified Green Pepper (Capsicum annuum) Pectin Methylesterase
authors: Castro, Sónia Marília
Van Loey, Ann
Saraiva, Jorge Alexandre
Smout, Chantal
Hendrickx, Marc
keywords: Capsicum annuum
pectin methylesterase
issue date: 2004
publisher: American Chemical Society
abstract: 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 °C was 7.5, and its optimum temperature at neutral pH was between 52.5 and 55.0 °C. 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 °C) and a biphasic model for higher temperatures (58?70 °C). The enzyme showed a stable behavior toward high-pressure/temperature treatments. Keywords: Capsicum annuum; pepper; pectin methylesterase; purification; characterization; thermal and high-pressure stability
URI: http://hdl.handle.net/10773/6973
ISSN: 0021-8561
publisher version/DOI: http://dx.doi.org/10.1021/jf0352071
source: Journal of Agricultural and Food Chemistry
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