Abstract
An acetyl esterase was purified from cell walls isolated from mung bean hypocotyls. The purified enzyme had an apparent M r of 43 300 and an apparent pI > 9. It rapidly deesterified triacetin and p-nitrophenylacetate and slowly released acetate from beet and flax pectins, the deesterification rate being increased by previous demethylation of the pectins. No significant peptide sequence identity between the acetyl esterase and any known protein could be found in protein data bases.
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