Characterization of a feruloyl esterase B from Talaromyces cellulolyticus |
| |
| Authors: | Masahiro Watanabe Erika Yoshida Hiroaki Fukada Hiroyuki Inoue Mitsunori Tokura |
| |
| Affiliation: | 1. Biomass Refinery Research Center, National Institute of Advanced Industrial Science and Technology (AIST), Higashi-hiroshima, Japan;2. Frontier Research Labs, Institute for Innovation Ajinomoto Co., Inc., Kawasaki, Japan |
| |
| 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. |
| |
| Keywords: | biomass fungus saccharification cellulase bagasse |
|
|
