Heterologous expression of two ferulic acid esterases from Penicillium funiculosum.
Two recombinant ferulic acid esterases from Penicillium funiculosum produced in Aspergillus awamori were evaluated for their ability to improve the digestibility of pretreated corn stover. The genes, faeA and faeB, were cloned from P. funiculosum and expressed in A. awamori using their native signal sequences. Both enzymes contain a catalytic domain connected to a family 1 carbohydrate-binding module by a threonine-rich linker peptide. Interestingly, the carbohydrate binding-module is N-terminal in FaeA and C-terminal in FaeB. The enzymes were purified to homogeneity using column chromatography, and their thermal stability was characterized by differential scanning microcalorimetry. We evaluated both enzymes for their potential to enhance the cellulolytic activity of purified Trichoderma reesei Cel7A on pretreated corn stover.
Knoshaug
Eric P
EP
National Bioenergy Center, National Renewable Energy Laboratory, Golden, CO 80401, USA. eric_knoshaug@nrel.gov
Selig
Michael J
MJ
Baker
John O
JO
Decker
Stephen R
SR
Himmel
Michael E
ME
Adney
William S
WS
D000327:Adsorption; D001230:Aspergillus / Q000235:genetics* / Q000378:metabolism*; D001665:Binding Sites; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D002482:Cellulose / Q000737:chemistry*; D004789:Enzyme Activation; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry; D010407:Penicillium / Q000145:classification / Q000235:genetics* / Q000378:metabolism*; D011485:Protein Binding; D015202:Protein Engineering / Q000379:methods; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D013045:Species Specificity; D013379:Substrate Specificity
D004800:Enzymes, Immobilized; D011994:Recombinant Proteins; D002482:Cellulose; D002265:Carboxylic Ester Hydrolases; C070196:feruloyl esterase