Activity and process stability of purified green pepper (Capsicum annuum) pectin methylesterase

被引:21
作者
Castro, SM
Van Loey, A
Saraiva, JA
Smout, C
Hendrickx, M
机构
[1] Katholieke Univ Leuven, Fac Appl Biosci & Engn, Lab Food Technol, B-3001 Heverlee, Belgium
[2] Univ Aveiro, Dept Chem, P-3810193 Aveiro, Portugal
关键词
Capsicum annuum; pepper; pectin methylesterase; purification; characterization; thermal and high-pressure stability;
D O I
10.1021/jf0352071
中图分类号
S [农业科学];
学科分类号
09 ;
摘要
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.
引用
收藏
页码:5724 / 5729
页数:6
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