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Purification of microbial b-galactosidase from Kluyveromyces fragilis by bioaffinity partitioning Rev. Microbiol.
Silva,Maria Estela da; Franco,Telma Teixeira.
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...
Tipo: Info:eu-repo/semantics/article Palavras-chave: B-galactosidase; Aqueous two-phase systems; Protein purification; Downstream-processing; Affinity.
Ano: 1999 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37141999000400006
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