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Cao,Qinghua; Li,Tao; Shao,Huanhuan; Tan,Xuemei; Zhang,Yizheng. |
Background: Zymomonas mobilis, as a novel platform for bio-ethanol production, has been attracted more attention and it is very important to construct vectors for the efficient expression of foreign genes in this bacterium. Results: Three shuttle vectors ( pSUZM 1, pSUZM2 and pSUZM3 ) were first constructed with the origins of replication from the chromosome and two native plasmids (pZZM401 and pZZM402) of Z. mobilis ZM4, respectively. The three shuttle vectors were stable in Z. mobilis ZM4 and have 3,32 and 27 copies, respectively. The promoter Ppdc (a), from the pyruvate decarboxylase gene, was clonedinto the shuttle vectors, generatingthe expressionvectors pSUZM1(2, 3)a. The codon-optimized glucoamylase gene from Aspergillus awamori combined with the... |
Tipo: Journal article |
Palavras-chave: Expression vector; Gene expression; Glucoamylase; Zymomonas mobilis. |
Ano: 2016 |
URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582016000100006 |
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Wang,Zhongshan; Xiang,Quanju; Wang,Guangjun; Wang,Haiyan; Zhang,Yizheng. |
The cloning, expression and purification of the glutathione (sulfur) import system ATP-binding protein (gsiA) was carried out. The coding sequence of Escherichia coli gsiA, which encodes the ATP-binding protein of a glutathione importer, was amplified by PCR, and then inserted into a prokaryotic expression vector pWaldo-GFPe harboring green fluorescent protein (GFP) reporter gene. The resulting recombinant plasmid pWaldo-GFP-GsiA was transformed into various E. coli strains, and expression conditions were optimized. The effect of five E. coli expression strains on the production of the recombinant gsiA protein was evaluated. E. coli BL21 (DE3) was found to be the most productive strain for GsiA-GFP fusion-protein expression, most of which was insoluble... |
Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Escherichia coli; Glutathione transporter; GsiA; Gene expression; Green fluorescent protein. |
Ano: 2011 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572011000400019 |
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