Expression of feruloyl esterase from Aspergillus awamori in Escherichia coli: Characterization and crystal studies of the recombinant enzyme.
This paper describes cloning, expression, characterization and crystallization of feruloyl esterase from Aspergillus awamori. The gene coding for feruloyl esterase from A. awamori was amplified, cloned, and expressed in Escherichia coli. The recombinant enzyme was purified, characterized and used for crystallization. Its X-ray crystallographic data were collected and explained using molecular replacement theory. Also, the tertiary structure of the recombinant enzyme-ferulic acid complex was also determined.
Fazary
Ahmed E
AE
Department of Chemical Engineering, National Taiwan University of Science and Technology, Taipei, Taiwan.
Hamad
Hamed A
HA
Lee
John C
JC
Koskei
Takuya
T
Lee
Cheng-Kang
CK
Ju
Yi-Hsu
YH
D001230:Aspergillus / Q000201:enzymology / Q000235:genetics*; D002265:Carboxylic Ester Hydrolases / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics* / Q000302:isolation & purification; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D004275:DNA, Ribosomal / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics*; D015870:Gene Expression; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics* / Q000302:isolation & purification
D004275:DNA, Ribosomal; D011994:Recombinant Proteins; D002265:Carboxylic Ester Hydrolases; C070196:feruloyl esterase