title: Expanded bed adsorption of an alkaline lipase from Pseudomona cepacia.
abstract: An extracellular lipase was isolated from Pseudomona cepacia by expanded bed adsorption on an Amberlite 410 ion-exchange resin. Enzyme characterization and hydrodynamic study of a chromatography column were done. Enzyme purification was done at three condition of expanded bed height (H): at one and half (6cm), at two (8cm) and at three (12cm) times the fixed bed height (H(0)=4cm). The results showed that the experimental data was fitted to the Richardson and Zaki equation, and the comparison between the experimental and calculated terminal velocities showed low relative error. In enzyme purification for better condition, a purification factor of about 80 times was found at 6cm of expanded bed height, or 1.5 times of expansion degree. Purified lipase had an optimal pH and a temperature of 8 and 37 degrees C, respectively.
authors.affiliation: Department of Engineering of Chemical Systems, School of Chemical Engineering, State University of Campinas, University Campus "Zeferino Vaz", Barão Geraldo, Campinas, SP, Brazil. giovana_padilha@yahoo.com.br
authors.forename: Giovana
authors.initials: G
authors.lastname: da Silva Padilha
authors.forename: José Carlos
authors.initials: JC
authors.lastname: Curvelo-Santana
authors.forename: Ranulfo Monte
authors.initials: RM
authors.lastname: Alegre
authors.forename: Elias Basile
authors.initials: EB
authors.lastname: Tambourgi
mesh_terms: D000327:Adsorption; D000468:Alkalies / Q000737:chemistry*; D001426:Bacterial Proteins / Q000032:analysis; D002021:Buffers; D016956:Burkholderia cepacia / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007475:Ion Exchange Resins / Q000737:chemistry; D008049:Lipase / Q000302:isolation & purification*; D000069463:Olive Oil; D010938:Plant Oils; D013696:Temperature
chemical_list: D000468:Alkalies; D001426:Bacterial Proteins; D002021:Buffers; D007475:Ion Exchange Resins; D000069463:Olive Oil; D010938:Plant Oils; D008049:Lipase