title: Purification and characterization of a feruloylesterase from Aspergillus awamori.
abstract: 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.
authors.affiliation: National Research Institute of Brewing, Higashi-Hiroshima, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Koseki
authors.forename: S
authors.initials: S
authors.lastname: Furuse
authors.forename: K
authors.initials: K
authors.lastname: Iwano
authors.forename: H
authors.initials: H
authors.lastname: Matsuzawa
mesh_terms: D001230:Aspergillus / Q000201:enzymology*; D002265:Carboxylic Ester Hydrolases / Q000302:isolation & purification* / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D011134:Polysaccharides / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D011134:Polysaccharides; C007916:hemicellulose; D002265:Carboxylic Ester Hydrolases; C070196:feruloyl esterase