Characterization of a feruloyl esterase B from <i>Talaromyces cellulolyticus</i>

<div><p>A feruloyl esterase catalyzes the hydrolysis of the 4-hydroxy-3-methoxycinnamoyl (feruloyl) group from esterified sugars in plant cell walls. <i>Talaromyces cellulolyticus</i> is a high cellulolytic-enzyme producing fungus. However, there is no report for feruloyl esterase activity of <i>T. cellulolyticus.</i> Analysis of the genome database of <i>T. cellulolyticus</i> identified a gene encoding a putative feruloyl esterase B. The recombinant enzyme was prepared using a <i>T. cellulolyticus</i> homologous expression system and characterized. The purified enzyme exhibited hydrolytic activity toward <i>p</i>-nitrophenyl acetate, <i>p</i>-nitrophenyl trans-ferulate, methyl ferulate, rice husk, and bagasse. HPLC assays showed that the enzyme released ferulic acid and <i>p</i>-coumaric acid from hydrothermal-treated rice husk and bagasse. <i>Trichoderma</i> sp. is well-known high cellulolytic-enzyme producing fungus useful for the lignocellulosic biomass saccharification. Interestingly, no feruloyl esterase has been reported from <i>Trichoderma</i> sp. The results show that this enzyme is expected to be industrially useful for biomass saccharification.</p>