Data/hora: 05/06/2024 04:48:32

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