Watanabe_2015_Biosci.Biotechnol.Biochem_79_1845

Reference

Title : Characterization of a feruloyl esterase B from Talaromyces cellulolyticus - Watanabe_2015_Biosci.Biotechnol.Biochem_79_1845
Author(s) : Watanabe M , Yoshida E , Fukada H , Inoue H , Tokura M , Ishikawa K
Ref : Biosci Biotechnol Biochem , 79 :1845 , 2015
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.

PubMedSearch : Watanabe_2015_Biosci.Biotechnol.Biochem_79_1845
PubMedID: 26110915
Gene_locus related to this paper: talce-faeB

Related information

Substrate p-coumaric-acid
Gene_locus p-coumaric-acid    talce-faeB

Citations formats

Watanabe M, Yoshida E, Fukada H, Inoue H, Tokura M, Ishikawa K (2015)
Characterization of a feruloyl esterase B from Talaromyces cellulolyticus
Biosci Biotechnol Biochem 79 :1845

Watanabe M, Yoshida E, Fukada H, Inoue H, Tokura M, Ishikawa K (2015)
Biosci Biotechnol Biochem 79 :1845