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Purification and properties of the major pectinesterases in lemon fruits ( Citrus limon )
Author(s) -
Macdonald Helen M,
Evans Roger,
Spencer Wendy J
Publication year - 1993
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/jsfa.2740620209
Subject(s) - pectinesterase , chemistry , sephadex , orange (colour) , citrus limon , enzyme , rutaceae , lipoxygenase , pectin , food science , chromatography , biochemistry , botany , pectinase , biology
Pectinesterase from lemon was separated into seven fractions by chromatography on CM‐Sephadex C‐50. Purification was hindered by the presence of pectin, for which the pectinesterase had a high affinity. Two major pectinesterases were purified: one was located solely in the peel and the other in the endocarp. They possessed similar molecular weights (35 kDa and 33 kDa, respectively) and high isoelectric points (> 11, and c 9). They required the presence of cations for optimal activity, the peel pectinesterase requiring a higher concentration of cations than the endocarp enzyme. Both enzymes were completely inactivated at temperatures above 88°C. Although neither enzyme destabilised the cloud of lemon juice or of comminuted lemon beverages, they caused cloud destabilisation of orange juice.