Characterization of enzymatically synthesized diferulate.
Horseradish peroxidase was used to synthesize diferulates by a procedure in which ethyl ferulate was used as substrate. Four different forms were obtained, of which two dominant were the 5-5' and 8-5' diferulate. Fluorescence emission spectra of the diferulates (excited at 284 nm) indicate that they contain two chromophores, as opposed to the substrate molecule. Fluorescence excitation spectra with emission at 417 nm further demonstrate the difference between the synthesized diferulates and starting substrates.
Tufegdzić
Srdhan
S
Institute of Chemistry, Technology and Metallurgy, Belgrade, Serbia and Montenegro. srdjant@chem.bg.ac.yu
Bogdanović
Jelena
J
Maksimović
Vuk
V
Vucinić
Zeljko
Z
D002109:Caffeic Acids / Q000737:chemistry; D002473:Cell Wall / Q000201:enzymology*; D003373:Coumaric Acids / Q000138:chemical synthesis* / Q000737:chemistry; D006735:Horseradish Peroxidase / Q000378:metabolism*; D007202:Indicators and Reagents; D008031:Lignin / Q000737:chemistry / Q000378:metabolism; D008956:Models, Chemical; D010944:Plants / Q000737:chemistry; D013050:Spectrometry, Fluorescence
D002109:Caffeic Acids; D003373:Coumaric Acids; D007202:Indicators and Reagents; C099085:ethyl ferulate; D008031:Lignin; C004999:ferulic acid; D006735:Horseradish Peroxidase