Purification and properties of the major pectinesterases in lemon fruits (Citrus limon)

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.