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Purification and changes in activities of tomato pectinesterase isoenzymes
Author(s) -
Tucker Gregory A.,
Robertson Neil G.,
Grierson Donald
Publication year - 1982
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.2740330415
Subject(s) - pectinesterase , ripening , isozyme , orange (colour) , chemistry , polyacrylamide gel electrophoresis , enzyme assay , enzyme , pectinase , horticulture , biochemistry , botany , biology , food science
Changes in the isoenzymes of pectinesterase were studied during the development of normal tomato fruit and of fruit from two near isogenic lines containing the ‘Never ripe’ ( Nr ) and ‘ripening inhibitor’ ( rin ) alleles. Nr fruit ripen slowly to an orange‐red while rin is even more extreme, eventually turning yellow. Enzyme activity present in normal green fruit increases during ripening, as did that in Nr fruit. No comparable increase was observed in rin fruit. Pectinesterase activity was resolved into two major forms by ion‐exchange chromatography. One of these isoenzymes (PE 2) accumulated during the ripening of normal and Nr fruit, but did not change in the rin fruit. PE 2 was purified to homogeneity, judged by electrophoresis in dodecyl sulphate‐polyacrylamide gels.