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http://hdl.handle.net/10773/6973
Title: | Activity and Process Stability of Purified Green Pepper (Capsicum annuum) Pectin Methylesterase |
Author: | Castro, Sónia Marília Van Loey, Ann Saraiva, Jorge Alexandre Smout, Chantal Hendrickx, Marc |
Keywords: | Capsicum annuum pepper pectin methylesterase purification characterization thermal |
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 |
Peer review: | yes |
URI: | http://hdl.handle.net/10773/6973 |
DOI: | 10.1021/jf0352071 |
ISSN: | 0021-8561 |
Appears in Collections: | QOPNA - Artigos |
Files in This Item:
File | Description | Size | Format | |
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P11_JAFC_PME activity.pdf | 119.44 kB | Adobe PDF | View/Open |
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