Journal
PROTEIN EXPRESSION AND PURIFICATION
Volume 115, Issue -, Pages 153-157Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.pep.2015.08.015
Keywords
Feruloyl esterase; Aspergillus terreus; Pichia pastoris; Lignocelluloses biodegradation
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Funding
- National Natural Science Foundation of China [31401542, 31271948, 31371850]
- Henan University of Technology [2012BS038]
- Key Laboratory of Environmental and Applied Microbiology, Chengdu Institute of Biology, Chinese Academy of Sciences [KLCAS-2013-06]
- Plan of Nature Science Fundamental Research in Henan University of Technology [2014JCYJ12]
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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. (C) 2015 Elsevier Inc. All rights reserved.
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