Sintesis de Lignanos mediante peroxidasas aisladas de Callos de Bupleurum salicifolium

  1. Juan Cristo Luis Jorge
  2. Francisco Valdés González
  3. Juan Ignacio Frías Viera
Majorensis: Revista Electrónica de Ciencia y Tecnología

ISSN: 1697-5529

Year of publication: 2010

Issue: 6

Pages: 10-15

Type: Article


A novel peroxidase that catalyses the transformation of caffeic acid and ferulic acid via oxidative coupling was purified from callus cultures of Bupleurum salicifolium petioles. The enzyme that was purified over 2900 fold is a glycoprotein with a molecular size of 38000, determined by SDS/PAGE and gel filtration. The Km values obtained were for caffeic 2.4 x 10-4 M and for ferulic acid 2.6 x 10-4 M while the Km values for H2O2 with caffeic acid was 4 x 10-5 M and for H2O2 with ferulic acid was 4.8 x 10-4 M. The purified peroxidase exhibits lower activity with typical peroxidase substrates (guaiacol and pyrogallol) than it does with caffeic and ferulic acids, but does not exhibit any activity on other phenylpropanoids tested (cinnamic acid, coumaric acid and 3, 4-dimetoxy cinnamic acid).