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Purification, properties and heat inactivation of pectin methylesterase from apple (cv Golden Delicious)
Author(s) -
Denès JeanMarc,
Baron Alain,
Drilleau JeanFrançois
Publication year - 2000
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/1097-0010(200008)80:10<1503::aid-jsfa676>3.0.co;2-u
Subject(s) - chemistry , pectin , pectinesterase , chromatography , isoelectric point , glycerol , pectin lyase , enzyme , sodium , food science , biochemistry , pectinase , organic chemistry
Pectin methylesterase from apple (cv Golden Delicious) was extracted and purified by affinity chromatography on a CNBr‐Sepharose®‐PMEI column. A single pectin methylesterase peak was observed. Isoelectric points were higher than 9. Kinetic parameters of the enzyme were determined as K m = 0.098 mg ml −1 and V max = 3.86 µmol min −1 ml −1 of enzyme. The optimum pH of the enzyme was above 7.5 and its optimum temperature was 63 °C. The purified PME required the presence of NaCl for optimum activity, and the sodium chloride optimum concentration increased with decreasing pH (from 0.13 M at pH 7 to 0.75 M at pH 4). The heat stability of purified PME was investigated without and with glycerol (50%), and thermal resistance parameters ( D and Z values) were calculated showing that glycerol improved the heat resistance of apple PME. © 2000 Society of Chemical Industry