Purification of a new peroxidase catalysing the formation of lignan-type compounds

• Published in: Biochemical journal Vol. 273; no. 1; pp. 109 - 113
• Main Authors: Frias, I, Siverio, J.M, Gonzalez, C, Trujillo, J.M, Perez, J.A
• Format: Journal Article
• Language: English
• Published: Colchester Portland Press 1991
• Subjects: Analytical, structural and metabolic biochemistry; Biological and medical sciences; biosynthesis; Bupleurum; bupleurum salicifolium; caffeate peroxidase; caffeic acid; Catalysis; catalytic activity; Chromatography, Gel; dimerization; Electrophoresis, Polyacrylamide Gel; Enzymes and enzyme inhibitors; ferulic acid; Fundamental and applied biological sciences. Psychology; glycoproteins; leaves; Lignans; Lignin - metabolism; Magnetic Resonance Spectroscopy; Mass Spectrometry; Oxidation-Reduction; Oxidoreductases; peroxidase; peroxidases; Peroxidases - isolation & purification; Peroxidases - metabolism; purification; Substrate Specificity; Characterization; Purification; Enzymatic activity; Molecular weight determination; Gel electrophoresis; Substrate specificity; Gel filtration; Peroxidase; NMR spectrometry; Kinetic parameter
• ISSN: 0264-6021; 1470-8728
• DOI: 10.1042/bj2730109

A novel peroxidase that catalyses the dimerization of ferulic acid or caffeic acid via oxidative coupling and formation of beta beta'-linkage to the lignan-type compounds 8,8'-bis(caffeic acid) or 8,8'-bis(ferulic acid) respectively was purified from the leaves of Bupleurum salicifolium. The enzyme, for which the name caffeate peroxidase is proposed, was purified 2700-fold. It is a glycoprotein and has an Mr of 38 000 as determined by gel filtration and SDS/PAGE. The Km values for ferulic acid and caffeic acid were 0.24 mm and for H2O2 0.04 mm with caffeic acid and 0.48 mm with ferulic acid. The purified peroxidase does not exhibit activity on other phenylpropanoids tested and has no detectable phenol oxidase or NADPH oxidase activity. The caffeate peroxidase could be involved in the biosynthesis of lignans.