Pectin methylesterase in Citrus bergamia R.: purification, biochemical characterisation and sequence of the exon related to the enzyme active site.

@article{Laratta2008PectinMI,
  title={Pectin methylesterase in Citrus bergamia R.: purification, biochemical characterisation and sequence of the exon related to the enzyme active site.},
  author={Bruna Laratta and Luigi De Masi and Paola Minasi and Alfonso Giovane},
  journal={Food chemistry},
  year={2008},
  volume={110 4},
  pages={829-37}
}
Three forms of pectin methylesterase (PME) were purified, from bergamot fruit (Citrus bergamia R.), to homogeneity by ion-exchange and affinity chromatography. The isoforms, named PME I, PME II and PME III, according their elution order on a heparin-sepharose column, were characterized for their relative molecular mass, activity kinetic parameters and thermostability. The molecular mass was estimated to be 42kDa for the three forms, and the apparent Km values for citrus pectin were 0.9mg/ml for… CONTINUE READING