Esterase specificity of patatin from two potato cultivars

摘要

'Deacute;sireacute;e' potato tubers contained about one-half the patatin of 'Kennebec', a typical commercial cultivar. The 'Deacute;sireacute;e' patatin, like that of 'Kennebec', copurified with esterase activity, but it consisted of only two major ionic forms and its ability to hydrolysep-nitrophenyl esters was relatively low. Despite these differences, the esterase of 'Deacute;sireacute;e' patatin was quite active toward other substrates. Patatin isoforms, separated by isoelectric focusing, had the same esterase substrate preference as the cultivar-specific patatin from which they were derived.