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Abstract
A feruloyl esterase catalyzes the hydrolysis of the 4-hydroxy-3-methoxycinnamoyl (feruloyl) group from esterified sugars in plant cell walls. Talaromyces cellulolyticus is a high cellulolytic-enzyme producing fungus. However, there is no report for feruloyl esterase activity of T. cellulolyticus. Analysis of the genome database of T. cellulolyticus identified a gene encoding a putative feruloyl esterase B. The recombinant enzyme was prepared using a T. cellulolyticus homologous expression system and characterized. The purified enzyme exhibited hydrolytic activity toward p-nitrophenyl acetate, p-nitrophenyl trans-ferulate, methyl ferulate, rice husk, and bagasse. HPLC assays showed that the enzyme released ferulic acid and p-coumaric acid from hydrothermal-treated rice husk and bagasse. Trichoderma sp. is well-known high cellulolytic-enzyme producing fungus useful for the lignocellulosic biomass saccharification. Interestingly, no feruloyl esterase has been reported from Trichoderma sp. The results show that this enzyme is expected to be industrially useful for biomass saccharification.
Graphical Abstract
HPLC assays showed that TcFaeB released ferulic acid from hydrothermal-treated rice husk, but less ferulic acid than p-coumaric acid from hydrothermal-treated bagasse.
Acknowledgments
We would like to thank Dr Tatsuya Fujii of our member at National Institute of Advanced Industrial Science and Technology for his kind suggestions. The differential scanning calorimetry experiments were conducted by Dr Harumi Fukada of the Graduate School of Life and Environmental Sciences, Osaka Prefecture University.
Notes
Abbreviations: TcFaeB, feruloyl esterase B from Talaromyces cellulolyticus; pNA, p-nitrophenyl acetate; pNF, p-nitrophenyl trans-ferulate; MFA, methyl ferulate.
