Journal
PREPARATIVE BIOCHEMISTRY & BIOTECHNOLOGY
Volume 35, Issue 3, Pages 231-241Publisher
TAYLOR & FRANCIS INC
DOI: 10.1081/PB-200065635
Keywords
Bupleurum salicifolium; Apiaceae; callus culture; peroxidase purification; caffeic acid; ferulic acid; dehydrocinnamic acid; cell wall
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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, which was purified over 2,900-fold, is a glycoprotein with a molecular weight of 38,000, determined by SDS/PAGE and gel filtration. The K-m values obtained were 2.4 x 10(-4) M for caffeic and 2.6 x 10(-4) M for ferulic acid, 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 with other phenylpropanoids tested (cinnamic acid, coumaric acid, and 3,4-dimethoxycinnamic acid).
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