dc.creatorFalco, ALP
dc.creatorDurrant, LR
dc.creatorFranco, TT
dc.date2000
dc.dateDEC
dc.date2014-07-30T14:18:43Z
dc.date2015-11-26T16:58:54Z
dc.date2014-07-30T14:18:43Z
dc.date2015-11-26T16:58:54Z
dc.date.accessioned2018-03-28T23:46:32Z
dc.date.available2018-03-28T23:46:32Z
dc.identifierBrazilian Journal Of Chemical Engineering. Brazilian Soc Chemical Eng, v. 17, n. 41824, n. 819, n. 825, 2000.
dc.identifier0104-6632
dc.identifierWOS:000165740000043
dc.identifier10.1590/S0104-66322000000400044
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/58473
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/58473
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1278050
dc.descriptionAlpha-galactosidase taken from a raw extract of Sesbania marginata legume seeds was purified by partitioning in aqueous two-phase systems (ATPS). Initially, galactomannan/dextran 2,000,000 systems were used for the purification, and the partition coefficients of alpha -galactosidase varied from 1.5 to 4.0. However, mass transport in these systems was poor due to the high viscosity of the employed polymers. Therefore, partitioning in polyethyleneglycol (PEG)/ sodium phosphate systems and the effect of sodium chloride upon the enzyme purification and the yield of a-galactosidase were also investigated. The purification achieved in a single-step was 5.7 with a recovery of 144% of a-galactosidase, possibly due to the removal of materials which inhibited a-galactosidase activity before the purification. The removal of the main protein contaminants and the highest yields were achieved in PEG 4,000/ sodium phosphate + 6% NaCl system at pH 5.0. Further purification by preparative on-exchange chromatography was also developed.
dc.description17
dc.description41824
dc.description819
dc.description825
dc.languageen
dc.publisherBrazilian Soc Chemical Eng
dc.publisherSao Paulo
dc.publisherBrasil
dc.relationBrazilian Journal Of Chemical Engineering
dc.relationBraz. J. Chem. Eng.
dc.rightsaberto
dc.sourceWeb of Science
dc.subjectalpha-galactosidase
dc.subjectlegume seeds
dc.subjectenzyme purification
dc.subjectaqueous two phase systems
dc.subjectAqueous 2-phase Systems
dc.subjectSingle Protein Property
dc.titlePurification of alpha-galactosidase from seeds of Sesbania marginata
dc.typeArtículos de revistas


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