title: Purification by expanded bed adsorption and characterization of an alpha-amylases FORILASE NTL from A. niger.
abstract: In this work the purification and biochemistry characterization of alpha-amylases from Aspergillus niger (FORILASE NTL) were studied. The effects of expansion degree of resin bed on enzyme purification by expanded bed adsorption (EBA) have also been studied. Residence time distributions (RTD) studies were done to achieve the optimal conditions of the amylases recovery on ion-exchange resin, and glucose solution was used as a new tracer. Results showed that height equivalent of the theoretical plates (HETP), axial dispersion and the Prandt number increased with bed height, bed voidage and linear velocity. The adsorption capacity of alpha-amylases, on the resin, increased with bed height and the best condition was at four-expansion degree. alpha-Amylase characterization showed that this enzyme has high affinity with soluble starch, good hydrolysis potential and molecular weight of 116 kDa.
authors.affiliation: Department of Chemical Engineering, Federal University of Sergipe, University City, Prof. José Aloísio de Campos, Av. Marechal Rondon, S/N, Rosa Elze, CEP: 49.100-000, São Cristóvão, SE, Brazil.
authors.forename: A L
authors.initials: AL
authors.lastname: Toledo
authors.forename: J B
authors.initials: JB
authors.lastname: Severo
authors.forename: R R
authors.initials: RR
authors.lastname: Souza
authors.forename: E S
authors.initials: ES
authors.lastname: Campos
authors.forename: J C C
authors.initials: JC
authors.lastname: Santana
authors.forename: E B
authors.initials: EB
authors.lastname: Tambourgi
mesh_terms: D000327:Adsorption; D001234:Aspergillus niger / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D006868:Hydrolysis; D008970:Molecular Weight; D000516:alpha-Amylases / Q000737:chemistry* / Q000378:metabolism
chemical_list: D000516:alpha-Amylases