Data/hora: 09/06/2024 03:38:38

Provedor de dados: 	69	
País: 	Chile	
Título: 	Heterologous expression, purification and refolding of an anti-listerial peptide produced by Pediococcus acidilactici K7	
Autores: 	Halami,Prakash M; Chandrashekar,Arun.	
Data: 	2007-10-01	
Ano: 	2007	
Palavras-chave: 	Fusion protein; Inclusion bodies; In vitro refolding; Pediocin PA-1; Pediococcus acidilactici; RP-HPLC.	
Resumo: 	The fusion protein, 6XHis-Xpress-PedA was constructed and expressed in Escherichia coli BL21 (DE3). The presence of a 12.8 kDa recombinant protein, localized in inclusion bodies (IBs) at high concentration, was confirmed by SDS-PAGE analysis and by western blotting using anti-His antibody. The rec-pediocin was purified by Nickel-nitrilotriacetic acid beads and refolded using 5 mM of &amp;#946;-mercaptoethanol along with 1 M glycine. Results indicated that the refolded rec-pediocin had an early elution profile in the RP-HPLC when compared to the unfolded protein and it exhibited biological activity against Listeria monocytogenes V7 which was approximately 25 times less active compared to native counterpart. The final yield of purified rec-pediocin was 3 mg/l of the culture and is estimated to be 8-10 times higher than the purification by conventional methods.	
Tipo: 	Journal article	
Idioma: 	Inglês	
Identificador: 	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582007000400009	
Editor: 	Pontificia Universidad Católica de Valparaíso	
Formato: 	text/html	
Fonte: 	Electronic Journal of Biotechnology  v.10 n.4 2007