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