Highly soluble and stable recombinant holo-phycocyanin alpha subunit expressed in Escherichia coli


Autoria(s): Liu, Shaofang; Chen, Huaxin; Qin, Song; Zhang, Weijie; Guan, Xiangyu; Lu, Yandu
Data(s)

15/12/2009

Resumo

C-phycocyanin (Cpc) is one of the phycobiliproteins with highly fluorescent and various pharmacological activities Holo-Cpc-alpha Subunit (holo-CpcA) expressed in Escherichia colt resulted in low yield and tended to aggregate after purification in this Study, we constructed a new plasmid coding holo-CpcA fused with hexahistidine and maltose-binding protein tag, which designated as HMCpcA. to Improve Its Solubility and stability without the Impairment of its spectra anti fluorescent properties HMCpcA was significantly more stable over time and a wider range of pH as compared to holo-CpcA. In addition. both the solubility and yields of HMCpcA increase significantly We here provided an example to demonstrate that MBP could also Improve the stability of the protein it fused while it has been reported as a soluble fusion partner before. This novel fluorescent protein will facilitate the large-scale production and be potentially applicable for the development Of fluorescent probes, as well as antioxidant agents (C) 2009 Elsevier B V. All rights reserved

C-phycocyanin (Cpc) is one of the phycobiliproteins with highly fluorescent and various pharmacological activities Holo-Cpc-alpha Subunit (holo-CpcA) expressed in Escherichia colt resulted in low yield and tended to aggregate after purification in this Study, we constructed a new plasmid coding holo-CpcA fused with hexahistidine and maltose-binding protein tag, which designated as HMCpcA. to Improve Its Solubility and stability without the Impairment of its spectra anti fluorescent properties HMCpcA was significantly more stable over time and a wider range of pH as compared to holo-CpcA. In addition. both the solubility and yields of HMCpcA increase significantly We here provided an example to demonstrate that MBP could also Improve the stability of the protein it fused while it has been reported as a soluble fusion partner before. This novel fluorescent protein will facilitate the large-scale production and be potentially applicable for the development Of fluorescent probes, as well as antioxidant agents (C) 2009 Elsevier B V. All rights reserved

Identificador

http://ir.qdio.ac.cn/handle/337002/2977

http://www.irgrid.ac.cn/handle/1471x/166143

Idioma(s)

英语

Fonte

Liu, Shaofang; Chen, Huaxin; Qin, Song; Zhang, Weijie; Guan, Xiangyu; Lu, Yandu.Highly soluble and stable recombinant holo-phycocyanin alpha subunit expressed in Escherichia coli,BIOCHEMICAL ENGINEERING JOURNAL,2009,48(1):58-64

Palavras-Chave #Biotechnology & Applied Microbiology; Engineering, Chemical #Maltose-binding protein #Phycocyanin-alpha subunit #Protein engineering #Recombinant protein #Chromatography #Recombinant protein production
Tipo

期刊论文