An extracellular feruloyl esterase from the culture filtrates of the isolated fungus Alternaria tenuissima was successfully purified to apparent homogeneity by anion-exchange and size-exclusion chromatography. Peptide fragments of purified enzyme (designated as AltFAE; molecular weight of 30.3 kDa determined by SDS-PAGE) were identified by mass spectrometry using a NanoLC-ESI-MS/MS system. Michaelis-Menten constants (KM) and catalytic efficiencies (kcat/KM) were determined for typical substrates of feruloyl esterase, and the lowest KM of 50.6 μM (i.e., the highest affinity) and the highest kcat/KM (3.1 × 105 s—1 M–1) were observed for methyl p-coumarate and methyl ferulate, respectively. Not least, AltFAE catalyzed conversion of lignocellulosic material (e.g. wood meal) to release hydroxycinnamic products, i.e. ferulic- and p-coumaric acids.