Paper Report for: Zhang_2015_Protein.Expr.Purif_115_153
Reference
Title: Expression of feruloyl esterase A from Aspergillus terreus and its application in biomass degradation Zhang SB, Wang L, Liu Y, Zhai HC, Cai JP, Hu YS Ref: Protein Expr Purif, 115:153, 2015 : PubMed
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.
        
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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 Purif115: 153-7
Zhang SB, Wang L, Liu Y, Zhai HC, Cai JP, Hu YS (2015) Protein Expr Purif115: 153-7