A novel protein from mung bean hypocotyl cell walls with acetyl esterase activity.

@article{Bordenave1995ANP,
  title={A novel protein from mung bean hypocotyl cell walls with acetyl esterase activity.},
  author={Marianne Bordenave and Ren{\'e}e J. Goldberg and Jean Claude Huet and J. C. Pernollet},
  journal={Phytochemistry},
  year={1995},
  volume={38 2},
  pages={315-9}
}
An acetyl esterase was purified from cell walls isolated from mung bean hypocotyls. The purified enzyme had an apparent Mr 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.