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Expression of feruloyl esterase A from Aspergillus terreus and its application in biomass degradation.

Authors :
Zhang, Shuai-Bing
Wang, Le
Liu, Yan
Zhai, Huan-Chen
Cai, Jing-Ping
Hu, Yuan-Sen
Source :
Protein Expression & Purification. Nov2015, Vol. 115, p153-157. 5p.
Publication Year :
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 ( At FaeA) was cloned from Aspergillus terreus and the recombinant At FaeA was constitutively expressed in Pichia pastoris . The SDS–PAGE analysis of purified At FaeA showed two protein bands owing to the different extent of glycosylation, and the recombinant At FaeA had an optimum temperature of 50 °C and an optimum pH of 5.0. The substrate utilization and primary sequence identity of At FaeA 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 Af FaeA. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
10465928
Volume :
115
Database :
Academic Search Index
Journal :
Protein Expression & Purification
Publication Type :
Academic Journal
Accession number :
109492603
Full Text :
https://doi.org/10.1016/j.pep.2015.08.015