Purification Of Microbial β-galactosidase From Kluyveromyces Fragilis By Bioaffinity Partitioning

dc.creatorDa Silva M.E.
dc.creatorFranco T.T.
dc.date1999
dc.date2015-06-30T15:18:46Z
dc.date2015-11-26T15:22:54Z
dc.date2015-06-30T15:18:46Z
dc.date2015-11-26T15:22:54Z
dc.date.accessioned2018-03-28T22:32:01Z
dc.date.available2018-03-28T22:32:01Z
dc.identifier
dc.identifierRevista De Microbiologia. , v. 30, n. 4, p. 324 - 331, 1999.
dc.identifier13714
dc.identifier
dc.identifierhttp://www.scopus.com/inward/record.url?eid=2-s2.0-22844448692&partnerID=40&md5=2ef5472ee42e3f6655b2db865db5a457
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/100844
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/100844
dc.identifier2-s2.0-22844448692
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1260426
dc.descriptionThis work investigated the partitioning of β-galactosidase from Kluyveromyces fragilis in aqueous two-phase systems (ATPS) by bioaffinity. PEG 4000 was chemically activated with thresyl chloride, and the biospecific ligand p-aminophenyl 1-thio-β-D-galactopyranoside (APGP) was attached to the activated PEG 4000. A new two-step method for extraction and purification of the enzyme β-galactosidase from Kluyveromyces fragilis was developed. In the first step, a system composed of 6% PEG 4000-APGP and 8% dextran 505 was used, where β-galactosidase was strongly partitioned to the top phase (K = 2,330). In the second step, a system formed of 13% PEG-APGP and 9% phosphate salt was used to revert the value of the partition coefficient of β-galactosidase (K = 2 x 10-5) in order to provide the purification and recovery of 39% of the enzyme in the bottom salt-rich phase.
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dc.description4
dc.description324
dc.description331
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dc.languageen
dc.publisher
dc.relationRevista de Microbiologia
dc.rightsaberto
dc.sourceScopus
dc.titlePurification Of Microbial β-galactosidase From Kluyveromyces Fragilis By Bioaffinity Partitioning
dc.typeArtículos de revistas


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