Purification and characterization of a feruloylesterase from Aspergillus awamori.
A feruloylesterase was purified from the extracellular broth of Aspergillus awamori grown on wheat bran culture. The purified enzyme gave a single band on SDS-polyacrylamide gel electrophoresis and isoelectric focusing, with an apparent M(r) of 35,000 and a pI of 3.8, respectively. The substrate specificity of the purified enzyme differed obviously from that of acetylesterase of A. awamori. The enzyme bound to microcrystalline cellulose.
Koseki
T
T
National Research Institute of Brewing, Higashi-Hiroshima, Japan.
Furuse
S
S
Iwano
K
K
Matsuzawa
H
H
D001230:Aspergillus / Q000201:enzymology*; D002265:Carboxylic Ester Hydrolases / Q000302:isolation & purification* / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D011134:Polysaccharides / Q000378:metabolism*; D013379:Substrate Specificity
D011134:Polysaccharides; C007916:hemicellulose; D002265:Carboxylic Ester Hydrolases; C070196:feruloyl esterase