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Provedor de dados:  Rev. Microbiol.
País:  Brazil
Título:  Purification of microbial b-galactosidase from Kluyveromyces fragilis by bioaffinity partitioning
Autores:  Silva,Maria Estela da
Franco,Telma Teixeira
Data:  1999-12-01
Ano:  1999
Palavras-chave:  B-galactosidase
Aqueous two-phase systems
Protein purification
Downstream-processing
Affinity
Resumo:  This work investigated the partitioning of b-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-b-D-galactopyranoside (APGP) was attached to the activated PEG 4000. A new two-step method for extraction and purification of the enzyme b-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 b-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 b-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.
Tipo:  Info:eu-repo/semantics/article
Idioma:  Inglês
Identificador:  http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37141999000400006
Editor:  Sociedade Brasileira de Microbiologia
Relação:  10.1590/S0001-37141999000400006
Formato:  text/html
Fonte:  Revista de Microbiologia v.30 n.4 1999
Direitos:  info:eu-repo/semantics/openAccess
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