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PARTIAL PURIFICATION AND CHARACTERIZATION OF PEACH PECTINESTERASE
Author(s) -
JAVERI H.,
WICKER L.
Publication year - 1991
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.1991.tb00159.x
Subject(s) - pectinesterase , chemistry , isoelectric focusing , chromatography , phosphate , isoelectric point , biochemistry , enzyme , pectinase
Pectinesterase (EC 3.1.1.11) was extracted from peaches (Prunus persica) and partially purified by preparative free solution isoelectric focusing. On SDS‐PAGE gels, protein bands at 36.3 and 33.9 kilodaltons represented the major bands; minor bands were observed at 108.4, 40.7, and 17.0 kilodaltons. The pH optimum for pectinesterase activity in the partially purified extract was 8.0. The enzyme was stable at 30°C for 30 min between pH values of 5 and 8. Peach pectinesterase is stable when heated at 55°C for 5 min in 0.1 M NaCl, 50 m M sodium phosphate, pH 7, buffer. However, residual activity decreased to 23% of 65°C for 5 min and was inactivated at 70°C for 5 min. The energy of activation of peach pectinesterase was determined to be 34, 600 J/mol °K. The Q 10 between 30°C and 60°C was estimated to be 1.5–1.6.