Sintesis de Lignanos mediante peroxidasas aisladas de Callos de Bupleurum salicifolium

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

ISSN: 1697-5529

Argitalpen urtea: 2010

Zenbakia: 6

Orrialdeak: 10-15

Mota: Artikulua

Beste argitalpen batzuk: Majorensis: Revista Electrónica de Ciencia y Tecnología

Laburpena

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).