| Title : Expression of feruloyl esterase A from Aspergillus terreus and its application in biomass degradation - Zhang_2015_Protein.Expr.Purif_115_153 |
| Author(s) : Zhang SB , Wang L , Liu Y , Zhai HC , Cai JP , Hu YS |
| Ref : Protein Expr Purif , 115 :153 , 2015 |
|
Abstract :
Feruloyl esterases (FAEs) are key enzymes involved in the complete biodegradation of lignocelluloses, which could hydrolyze the ester bonds between hemicellulose and lignin. The coding sequence of a feruloyl esterase A (AtFaeA) was cloned from Aspergillus terreus and the recombinant AtFaeA was constitutively expressed in Pichia pastoris. The SDS-PAGE analysis of purified AtFaeA showed two protein bands owing to the different extent of glycosylation, and the recombinant AtFaeA had an optimum temperature of 50 degrees C and an optimum pH of 5.0. The substrate utilization and primary sequence identity of AtFaeA demonstrated that it is a type-A feruloyl esterase. The hydrolysis of corn stalk and corncob by xylanase from Aspergillus niger could be significantly improved in concert with recombinant AfFaeA. |
| PubMedSearch : Zhang_2015_Protein.Expr.Purif_115_153 |
| PubMedID: 26282562 |
Zhang SB, Wang L, Liu Y, Zhai HC, Cai JP, Hu YS (2015)
Expression of feruloyl esterase A from Aspergillus terreus and its application in biomass degradation
Protein Expr Purif
115 :153
Zhang SB, Wang L, Liu Y, Zhai HC, Cai JP, Hu YS (2015)
Protein Expr Purif
115 :153