Registro completo |
Provedor de dados: |
Rev. Microbiol.
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País: |
Brazil
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Título: |
Purification of microbial b-galactosidase from Kluyveromyces fragilis by bioaffinity partitioning
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Autores: |
Silva,Maria Estela da
Franco,Telma Teixeira
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Data: |
1999-12-01
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Ano: |
1999
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Palavras-chave: |
B-galactosidase
Aqueous two-phase systems
Protein purification
Downstream-processing
Affinity
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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.
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Tipo: |
Info:eu-repo/semantics/article
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Idioma: |
Inglês
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Identificador: |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37141999000400006
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Editor: |
Sociedade Brasileira de Microbiologia
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Relação: |
10.1590/S0001-37141999000400006
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Formato: |
text/html
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Fonte: |
Revista de Microbiologia v.30 n.4 1999
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Direitos: |
info:eu-repo/semantics/openAccess
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