Data/hora: 05/06/2024 01:15:58

Provedor de dados: | 59
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
Fonte: | info:eu-repo/semantics/openAccess